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1.
J Clin Invest ; 92(5): 2368-76, 1993 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-8227353

RESUMEN

The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ (GHK-Cu) was first described as a growth factor for differentiated cells. Recent in vitro data showed that it possesses several properties of a potential activator of wound repair. We investigated the effects of GHK-Cu in vivo, using the wound chamber model described previously (Schilling, J.A., W. Joel, and M.T. Shurley, 1959. Surgery [St. Louis]. 46:702-710). Stainless steel wire mesh cylinders were implanted subcutaneously on the back of rats. The animals were divided into groups that received sequential injections into the wound chamber of either saline (control group) or various concentrations of GHK-Cu. At the end of the experiments, rats were killed, wound chambers were collected, and their content was analyzed for dry weight, total proteins, collagen, DNA, elastin, glycosaminoglycans, and specific mRNAs for collagens and TGF beta. In the GHK-Cu-injected wound chambers, a concentration-dependent increase of dry weight, DNA, total protein, collagen, and glycosaminoglycan contents was found. The stimulation of collagen synthesis was twice that of noncollagen proteins. Type I and type III collagen mRNAs were increased but not TGF beta mRNAs. An increase of the relative amount of dermatan sulfate was also found. A control tripeptide, L-glutamyl-L-histidyl-L-proline, had no significant effect. These results demonstrate that GHK-Cu is able to increase extracellular matrix accumulation in wounds in vivo.


Asunto(s)
Tejido Conectivo/crecimiento & desarrollo , Cobre/farmacología , Sustancias de Crecimiento/farmacología , Oligopéptidos/farmacología , Piel/lesiones , Cicatrización de Heridas/efectos de los fármacos , Animales , Colágeno/biosíntesis , Colágeno/genética , Tejido Conectivo/efectos de los fármacos , Dermatán Sulfato/biosíntesis , Cámaras de Difusión de Cultivos , Relación Dosis-Respuesta a Droga , Expresión Génica/efectos de los fármacos , Masculino , ARN Mensajero/análisis , Ratas , Ratas Sprague-Dawley
2.
Biochim Biophys Acta ; 1039(2): 189-96, 1990 Jun 19.
Artículo en Inglés | MEDLINE | ID: mdl-2364094

RESUMEN

Two 140 kDa collagenous glycoproteins were isolated from 5 M guanidinium chloride extracts of human uterine leiomyoma by two-dimensional preparative gel electrophoresis. The glycoproteins represented the major concanavalin A binding fraction of the extract and were also present in adult human skin. On two-dimensional gel electrophoresis the glycoproteins appeared as elongated spots, indicating variations of their isoelectric points from 5 to 6. These glycoproteins were disulfide-bonded components of high molecular mass protein and, after reduction, became sensitive to collagenase treatment that generated peptides corresponding in size to those of the noncollagenous domains of type VI collagen. Antisera raised against these purified glycoproteins reacted with either pepsin-derived alpha 1(VI) or pepsin-derived alpha 2(VI) chains but not with alpha 3(VI) chain of human type VI collagen. Reciprocally, these glycoproteins reacted with monoclonal antibodies against type VI collagen. These results indicate that the glycoproteins represent the integral alpha 1 and alpha 2 chains of type VI collagen. The globular domains of alpha 1(VI) and alpha 2(VI) chains remaining after collagenase treatment appeared on two-dimensional gel electrophoresis as elongated spots, suggesting that the noncollagenous portions determine the well known microheterogeneity of the molecule. The differences in isoelectric points between and within alpha chains may facilitate the formation of microfibrillar network.


Asunto(s)
Colágeno/aislamiento & purificación , Aminoácidos/análisis , Anticuerpos Monoclonales , Electroforesis en Gel Bidimensional/métodos , Electroforesis en Gel de Poliacrilamida/métodos , Femenino , Guanidina , Guanidinas , Humanos , Leiomioma/análisis , Sustancias Macromoleculares , Peso Molecular , Embarazo , Piel/análisis , Neoplasias Uterinas/análisis
3.
FEBS Lett ; 357(3): 287-9, 1995 Jan 09.
Artículo en Inglés | MEDLINE | ID: mdl-7835429

RESUMEN

Fibroblasts cultivated in three-dimensional lattices exhibit a large decrease of protein synthesis, mainly through transcriptional control. However, no previous work was devoted to a potential ribosomal regulation. We evaluated ribosomal ribonucleic acid (RNA) in monolayer- and collagen lattice-cultured fibroblasts. After one week of culture, total RNA was 60% lower in lattice-cultured fibroblasts than in monolayer-cultured cells. The decrease was identical for 18 S and 28 S rRNA subfractions. The half-life of RNA was much shorter in collagen lattice-cultured fibroblasts than in monolayers. These results suggest that protein synthesis in lattice-cultured fibroblasts is partly regulated at the ribosomal level.


Asunto(s)
Colágeno/metabolismo , Biosíntesis de Proteínas , Ribosomas/metabolismo , Adulto , Células Cultivadas , Fibroblastos/metabolismo , Humanos , ARN Ribosómico/metabolismo
4.
Biochem Pharmacol ; 33(21): 3491-7, 1984 Nov 01.
Artículo en Inglés | MEDLINE | ID: mdl-6497905

RESUMEN

Rabbits were fed with normal (group 1 and 2) and cholesterol rich diets (group 3 and 4) concomitantly to a daily peroral administration of 50 mg/kg procyanidolic oligomers (PCO) to groups 2 and 4. After 10 weeks, the cholesterol content of the blood serum and the excised aortic intima-media were significantly higher in groups 3 and 4 than in groups 1 and 2. The DNA, hydroxyproline, uronic acid contents were similar in aortic dry weight basis in all four groups. The intima-media samples were extracted successively with 0.15 M NaCl, 0.02 M sodium phosphate pH 7.4 (NaCl extract) and with 4 M guanidinium chloride, 0.05 M sodium acetate pH 5.8 prior (G1 extract) and following (G2 extract) hydrolysis of the collagen with collagenase. The cholesterol contents of G1 extracts were higher in groups 2 and 4 than in groups 1 and 3. The cholesterol content of aortic elastin increased with cholesterol feeding (group 3). With simultaneous administration of cholesterol and PCO the cholesterol content of aortic elastin in group 4 was significantly lower than in group 3. The uronic acid contents increased in G1 extracts and in the collagenase digest with PCO treatment of both normal and hypercholesterolemic rabbits. The ratio of dermatan-sulphate to chondroitin-sulphate decreased with hypercholesterolemia (group 3) and with PCO (group 2 and 4). The parallelism between increased cholesterol and uronic acid contents and modified glycosaminoglycan composition in G1 extract, indicate that the interaction of cholesterol with macromolecules of the aorta can be modulated by PCO. This drug modifies the extractibility of aortic cholesterol and glycosaminoglycans and reduces the association of cholesterol to elastin.


Asunto(s)
Aorta/efectos de los fármacos , Benzopiranos/farmacología , Biflavonoides , Catequina/farmacología , Hipercolesterolemia/metabolismo , Proantocianidinas , Animales , Aorta/análisis , Colesterol/análisis , Colesterol/sangre , Glicosaminoglicanos/análisis , Masculino , Proteínas/análisis , Conejos , Ácidos Urónicos/análisis
5.
Radiat Res ; 125(1): 14-9, 1991 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-1986396

RESUMEN

Collagen metabolism was investigated in the fibrotic tissue which developed in pig thigh muscle 6 to 15 months after acute gamma irradiation. During this period, total collagen deposits in the fibrotic tissue increased 10-fold compared to the healthy muscle tissue. These deposits were composed mainly of type I and III collagen, and the type I/type III ratio was lower in the fibrotic than in the muscle tissue. Small pieces of both fibrotic and muscle tissue were incubated with [14C]proline. The [14C]hydroxyproline content of the fibrotic tissue reflected large concomitant increases in the synthesis of total collagen, mainly of types I and III, which rose 14- and 17-fold, respectively. Similarly, the level of type I and type III procollagen mRNAs rose 9- and 5-fold, respectively, in the fibrotic tissue versus the muscle tissue. These results suggest that procollagen gene transcription or RNA maturation in the cell nuclei is activated in the fibrotic tissue. The possibility that such activation is due to the long-term inflammatory state of this tissue is discussed.


Asunto(s)
Colágeno/biosíntesis , Músculos/efectos de la radiación , Animales , Fibrosis , Rayos gamma , Radioisótopos de Iridio , Músculos/metabolismo , Músculos/patología , ARN Mensajero/análisis , Porcinos , Factores de Tiempo
6.
Int J Radiat Biol ; 61(5): 685-93, 1992 May.
Artículo en Inglés | MEDLINE | ID: mdl-1349633

RESUMEN

The content and biosynthesis of glycosaminoglycans (GAGs) were studied in the pig thigh muscle after acute local gamma-irradiation. Seven months following irradiation, the muscular tissue next to the irradiation cone was replaced by severe mutilating fibrosis delimited by an intermediary perifbrotic zone. Fibrosis, perifibrotic tissue and normal muscle, were sampled and incubated with [3H]glucosamine and [35S]sulphate, and GAGs were isolated following pronase digestion. Results showed a parallel increase of collagen and GAG content in perifibrotic and fibrotic tissues. Sulphated GAGs, heparan sulphate and dermatan sulphate were preferentially accumulated in fibrotic tissue, while the hyaluronic acid content increased only slightly. Synthesis of sulphated GAGs was more elevated in fibrotic tissue than in perifibrotic zone as compared with normal muscle. Seven months after irradiation well-developed fibrotic tissue continued to synthesize and to accumulate extracellular matrix macromolecules, indicating the invasive aspect of post-irradiation fibrosis.


Asunto(s)
Glicosaminoglicanos/biosíntesis , Músculos/efectos de la radiación , Animales , Fibrosis , Masculino , Músculos/metabolismo , Músculos/patología , Porcinos , Muslo
7.
Int J Biol Macromol ; 12(3): 213-7, 1990 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-2271493

RESUMEN

The aortic proteoglycans and heparin were shown to form insoluble complexes with human low density lipoproteins (LDL). The effect of temperature, polyethylene glycol and ionic strength on the formation of complexes between porcine aortic proteodermatan sulphate (PDS) and LDL has been studied by laser nephelometry and comparisons made with heparin LDL complexes. Turbidity was a nonlinear function of the quantity of LDL precipitated by PDS. The turbidity of aggregates was constant at temperatures between 2 degrees C and 30 degrees C but increased with temperature above 30 degrees C up to 50 degrees C. The formation of insoluble complexes decreased rapidly with increasing NaCl concentration. Polyethylene glycol enhanced the turbidity at 20 degrees C but not at 37 degrees C. It also increased the resistance of complexes to dissociation by increasing ionic strength. The turbidity of heparin--LDL complexes was linearly correlated with the quantity of precipitated LDL. The heparin-LDL aggregates were less sensitive to modification of temperature and ionic strength than the PDS-LDL aggregates. These results suggest that ionic interactions are weaker in PDS-LDL complexes than in the heparin-LDL complexes. Non-coulombic interactions and/or temperature dependent conformational changes may be involved in the stabilization of supramolecular PDS-LDL aggregates. No such interactions or changes appear to be involved in complex formation between heparin and LDL.


Asunto(s)
Dermatán Sulfato/análogos & derivados , Heparina/química , Lipoproteínas LDL/química , Proteoglicanos/química , Animales , Aorta , Precipitación Química , Dermatán Sulfato/química , Humanos , Concentración Osmolar , Polietilenglicoles , Tiburones , Cloruro de Sodio , Porcinos , Temperatura
8.
Presse Med ; 21(41): 1951-3, 1992 Dec 02.
Artículo en Francés | MEDLINE | ID: mdl-1294948

RESUMEN

Interstitial renal fibrosis and gingival hypertrophy are frequent side-effects of cyclosporin A which have been attributed to a dysfunction of extracellular matrix synthesis. Endothelial cells might participate in the matrix accumulation observed. We studied the effects of increasing concentrations of cyclosporin A on protein synthesis by human umbilical vein endothelial cells. Collagen synthesis decreased significantly to 800 ng/ml in both medium and cell layer. The percentage of hydroxylation of its proline residues decreased significantly as from 400 ng/ml. The main proteins, analysed by SDS-PAGE, were thrombospondin, fibronectin and the alpha 1 and alpha 2 chains of type IV collagen. These fractions did not show any change after 24 hours exposure to 200 ng/ml of cyclosporin A. These results demonstrate an inhibitory effect of cyclosporin A on collagen synthesis by human umbilical vein endothelial cells. Consequently, matrix accumulation by increased collagen synthesis in cyclosporin A treated patient may not be directly related to the drug effect on endothelial cells.


Asunto(s)
Colágeno/biosíntesis , Ciclosporina/farmacología , Endotelio Vascular/metabolismo , Venas Umbilicales/metabolismo , Depresión Química , Endotelio Vascular/efectos de los fármacos , Humanos , Técnicas In Vitro , Venas Umbilicales/efectos de los fármacos
9.
Med Pr ; 31(1): 13-9, 1980.
Artículo en Polaco | MEDLINE | ID: mdl-7374431

RESUMEN

Female Wistar rats were exposed to CS2 for 13 months. Afterwards collagen and elastin content in aorta and lungs was determined. In addition, collagen and non-collagen protein biosynthesis was determined using 14-C glycine incorporation to proteins. Collagen and elastin content in aorta wall and elastin concentration in lungs were found to be increased. Isotopic method indicated that the specific activity of collagen in aorta wall was increased and activity of pulmonary collagen and non-collagen proteins of aorta and lungs was decreased. The above is indicative of: lowered biosynthesis of noncollagen proteins of aorta and lungs, increased biosynthesis of aorta collagen and increased biosynthesis of aorta and lung elastin. Increased biosynthesis of collagen and elastin in aorta may suggest a possibility of CS2 atherogenic effects.


Asunto(s)
Aorta/metabolismo , Disulfuro de Carbono/envenenamiento , Tejido Conectivo/metabolismo , Pulmón/metabolismo , Animales , Arteriosclerosis/inducido químicamente , Enfermedad Crónica , Colágeno/metabolismo , Elastina/metabolismo , Femenino , Ratas , Estimulación Química
10.
Med Pr ; 31(4): 311-8, 1980.
Artículo en Polaco | MEDLINE | ID: mdl-7442539

RESUMEN

In the studies carried out lipids content in blood serum and aorta wall as well as morphological changes in coronary vessels of CS2 exposed rats have been evaluated. The 10-month-exposure to CS2 at a concentration of 0,8--0,9 mg/l has been found to result in: (1) increased concentration of total and free cholesterol, cholesterol esters, triglycerides and phospholipids in blood serum; (2) increase in total cholesterol and significant rise in the level of cholesterol esters in the aorta wall; (3) a relative increase in serum VLDL, LDL and decrease in HDL fraction. Histological estimation has demonstrated in serial sections of hearts of the CS2 exposed animals thickened walls of left coronary artery branches with no lipid deposits. In two animals focal steatosis of aortic bulb wall and aortic valves and lipids droplets in endothelium of ascending aorta and coronary vessels have been found.


Asunto(s)
Aorta/metabolismo , Disulfuro de Carbono/envenenamiento , Metabolismo de los Lípidos , Animales , Aorta Torácica/metabolismo , Arteriosclerosis/inducido químicamente , Colesterol/metabolismo , Enfermedad Crónica , Lipoproteínas/metabolismo , Fosfolípidos/metabolismo , Conejos , Triglicéridos/metabolismo
12.
Biochem J ; 235(3): 823-31, 1986 May 01.
Artículo en Inglés | MEDLINE | ID: mdl-3753448

RESUMEN

Different proteoglycans (PGs) were isolated from pig aorta for aggregation studies with hyaluronic acid and human low-density lipoproteins (LDL). Extraction of the intima-media with 4M-guanidinium chloride and digestion of the residue with collagenase solubilized 91% of aortic hexuronic acid content. From the guanidinium chloride extract two PGs were isolated by ion-exchange and gel-permeation chromatography: proteochondroitin sulphate (PGI) with a protein-core apparent Mr of 250 000 and proteodermatan-chondroitin sulphate (PGII) with a protein-core apparent Mr of 55 000. Only PGI forms high-Mr aggregates with hyaluronic acid. From the collagenase digest two other PGs were isolated: proteoheparan sulphate and proteochondroitin sulphate (PGIII and PGIV respectively). PGIV had a smaller hydrodynamic size than PGI. PGI and PGII formed insoluble complexes with human LDL in the presence of Ca2+. PGIII or PGIV did not form precipitates with the LDL. PGI and PGII, but neither PGIII nor PGIV, were bound to LDL-Sepharose. The main peaks of PGI and PGII were eluted from LDL-Sepharose with 60 mM- and 90 mM-NaCl respectively. The results indicate that aortic PGs have different interacting potentials with lipoproteins, depending on their Mr and their glycosaminoglycan composition.


Asunto(s)
Aorta/metabolismo , Lipoproteínas LDL/metabolismo , Proteoglicanos/metabolismo , Animales , Cromatografía , Cromatografía en Gel , Glicosaminoglicanos/análisis , Ácido Hialurónico/metabolismo , Sustancias Macromoleculares , Unión Proteica , Proteoglicanos/aislamiento & purificación , Porcinos
13.
Connect Tissue Res ; 23(4): 237-49, 1989.
Artículo en Inglés | MEDLINE | ID: mdl-2698315

RESUMEN

Synthesis of fibronectin and glycosamingoglycans (GAGs) was studied in fibroblasts from pigs with post-irradiation subcutaneous fibrosis. Fibrosis was developed in the femoral muscle by local gamma irradiation with a dose of 60 Gy. Normal fibroblasts were obtained from the healthy skin of the same animal. To measure GAG and fibronectin synthesis fibrotic and normal fibroblasts were labeled with 3H-glucosamine, 35S-sulfate and 35S-methionine. Fibrotic fibroblasts synthesized 2.5 times as much fibronectin as normal skin fibroblasts but total protein synthesis did not change. Parallel enhanced secretion of hyaluronic acid and dermatan sulfate into the cell culture medium were also observed. GAGs from the pericellular layer of trypsin-digested fibrotic fibroblasts exhibited increased 3H incorporation, but reduced 35S-sulfate incorporation. The largest reduction in the latter was observed for heparan sulfate. These results indicate that the fibroblasts from the well developed fibrotic tissue maintain enhanced synthesis of matrix macromolecules in primary cultures. Structural and/or metabolic changes in secreted GAGs, combined with the stimulation of tissue repair by growth factors may be responsible for the excessive deposition of collagen in post-irradiation fibrosis.


Asunto(s)
Fibroblastos/citología , Fibronectinas/metabolismo , Glicosaminoglicanos/metabolismo , Animales , Células Cultivadas , Fibroblastos/metabolismo , Fibrosis/metabolismo , Fibrosis/patología , Técnica del Anticuerpo Fluorescente , Porcinos
14.
Cell Biol Int Rep ; 13(10): 881-90, 1989 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-2805078

RESUMEN

The effects of thyroid-stimulating hormone (TSH) and a tumor promoter: 12-0-tetradecanoyl-phorbol-13-acetate on glycosaminoglycan (GAG) synthesis were studied in porcine thyroid epithelial cells in primary culture. TSH is known to involve cyclic AMP mechanism and phorbol ester to act by protein kinase C pathway. Chronic treatment of cells with TSH increased the synthesis of heparan sulphate associated with the cell layer and hyaluronic acid in the culture medium. Phorbol ester increased the radioactivity of total GAGs in the culture medium but had no effect on GAGs associated with the cell layer. It inhibited the positive effect of TSH on heparan sulphate synthesis. These results suggest that in thyroid epithelial cells the synthesis of the GAGs associated with the cell layer and those secreted into the culture medium are regulated by different intracellular mechanisms.


Asunto(s)
Glicosaminoglicanos/biosíntesis , Acetato de Tetradecanoilforbol/farmacología , Glándula Tiroides/metabolismo , Tirotropina/farmacología , Animales , Células Cultivadas , Epitelio/metabolismo , Glucosamina/metabolismo , Heparitina Sulfato/biosíntesis , Ácido Hialurónico/biosíntesis , Sulfatos/metabolismo , Radioisótopos de Azufre , Porcinos , Glándula Tiroides/efectos de los fármacos , Tritio
15.
Exp Mol Pathol ; 48(3): 273-85, 1988 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-3371453

RESUMEN

Six months after acute local gamma irradiation of the pig skin and adjacent muscle, the muscular tissue is replaced by a large mutilating and proliferative fibrosis deliminated by a perifibrotic inflammatory zone. The content and biosynthesis of collagen and noncollagenous proteins were studied in both fibrotic and perifibrotic zones after incubation of the biopsies with [14C]proline or [35S]methionine for 24 hr. Cells of perifibrotic and fibrotic regions synthesize about 10 times more proteins than those in the nonirradiated muscle. When compared to normal muscle tissue, our results indicate an important increase in collagen content and biosynthesis in fibrotic tissue. The increase in collagen biosynthesis in the irradiated tissue is more pronounced for type III collagen than for type I collagen. Biosynthesis of type III and type I collagens increases 20- and 10-fold, respectively, compared to the normal muscle. Type I to III collagen ratio in irradiated tissue decreases from 2.3 in normal tissue to 1.1 in fibrotic tissue. Histological examination of the biopsies as well as the protein pattern by polyacrylamide gel electrophoresis show striking differences in the perifibrotic and fibrotic areas as compared to the normal muscular tissue with a progressive disappearance of the myotubes replaced by a dense sclerotic tissue. The results indicate that the perifibrotic inflammatory area is engaged in a remodeling process and that the fibrotic tissue remains active in the neosynthesis of the extracellular matrix macromolecules with a high proportion of type III collagen. This high biosynthetic activity of the irradiated tissue may explain the pseudosarcomatous character of the radiation-induced lesions.


Asunto(s)
Colágeno/metabolismo , Enfermedades Musculares/metabolismo , Proteínas/metabolismo , Traumatismos Experimentales por Radiación/metabolismo , Animales , Fibrosis , Rayos gamma/efectos adversos , Inflamación , Masculino , Enfermedades Musculares/etiología , Enfermedades Musculares/patología , Porcinos
16.
Clin Physiol Biochem ; 3(5): 226-33, 1985.
Artículo en Inglés | MEDLINE | ID: mdl-3902320

RESUMEN

The biosynthesis of proteins and glycosaminoglycans (GAGs) was determined in skin biopsies from atherosclerotic patients treated perorally for 3 months with 1 mg/day colchicine. The biopsies were incubated with 3H-glucosamine and 14C-proline for 5 h and subsequently digested with pronase. In an aliquot of the pronase digest, the specific radioactivity of 14C-proline and 14C-hydroxyproline were determined. The 3H-glucosamine-labeled GAGs were identified by specific enzymic assay and quantified after electrophoretic separation. 3 months treatment with colchicine did not modify the total amounts of proline and hydroxyproline in skin proteins, but diminished the amount of the GAGs as expressed by uronic acid content. Colchicine treatment decreased also the specific radioactivity of proline and hydroxyproline, which reflects a decrease of total protein and collagen synthesis. The incorporation of 3H-glucosamine in the 3H-GAGs was also decreased, mainly in hyaluronic acid. These results suggest that peroral administration of colchicine modifies the synthesis of extracellular matrix proteins and polysaccharides by skin fibroblasts.


Asunto(s)
Arteriosclerosis/metabolismo , Colchicina/uso terapéutico , Glicosaminoglicanos/biosíntesis , Biosíntesis de Proteínas , Piel/metabolismo , Adulto , Anciano , Arteriosclerosis/tratamiento farmacológico , Biopsia , Ensayos Clínicos como Asunto , Femenino , Humanos , Hidroxiprolina/análisis , Cinética , Masculino , Persona de Mediana Edad , Prolina/análisis , Piel/efectos de los fármacos , Piel/patología , Ácidos Urónicos/análisis
17.
Clin Physiol Biochem ; 5(2): 61-9, 1987.
Artículo en Inglés | MEDLINE | ID: mdl-3621792

RESUMEN

A study of the behavior of plasma fibronectin during a radiation-induced inflammatory lung reaction was carried out. Rats were exposed to a single homogenous thoracic irradiation of 15 Gy from a 60Co gamma source. Perchlorosoluble glycoproteins were determined (as sialic acid) as well as plasma fibronectin at 2, 8, 27, 60 and 120 days after irradiation. A parallel increase of the perchlorosoluble glycoproteins and plasma fibronectin was found. Morphological and histological studies of the irradiated lungs showed a predominating endothelial cell injury in the lung microcapillaries. The parallel increase of plasma fibronectin and perchlorosoluble serum glycoproteins suggests that plasma fibronectin can be considered as an acute phase reactant. Its early increase may be the result of the inflammatory reaction and endothelial injury induced by the radiation.


Asunto(s)
Fibronectinas/sangre , Glicoproteínas/sangre , Pulmón/efectos de la radiación , Traumatismos Experimentales por Radiación/sangre , Animales , Pulmón/patología , Masculino , Ácido N-Acetilneuramínico , Fibrosis Pulmonar/sangre , Ratas , Ratas Endogámicas , Ácidos Siálicos/sangre , Solubilidad
18.
Exp Cell Res ; 205(2): 426-9, 1993 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-8482349

RESUMEN

After separation of the various alpha chains of the collagens by SDS-PAGE, the binding of polymorphonuclear neutrophils (PMN) to these chains was detected by a double-antibody technique and the activation of PMN by nitro blue tetrazolium. All of the alpha chains tested were able to bind PMNs. The alpha 1 chain of type I collagen activated the PMN when it had not been treated with pepsin. Pepsinized types II and VI collagens did not activate PMN. The pepsinized alpha 1(III) chains and all three alpha chains from pepsinized type V collagen were able to activate PMN.


Asunto(s)
Adhesión Celular , Colágeno/metabolismo , Neutrófilos/citología , Colágeno/aislamiento & purificación , Electroforesis en Gel de Poliacrilamida , Humanos , Técnicas In Vitro , Neutrófilos/metabolismo , Nitroazul de Tetrazolio/metabolismo
19.
Anal Biochem ; 175(1): 263-73, 1988 Nov 15.
Artículo en Inglés | MEDLINE | ID: mdl-3245573

RESUMEN

A method of extraction of the collagen and noncollagen proteins from deep dermis of young adult rabbits using a 0.1 M tartaric acid solution was set up. The tartaric acid extraction, together with the preliminary neutral salt extraction, solubilized 95% of the total collagen and 98% of the noncollagen proteins, far more than the 6 M guanidinium Cl solution used for comparison. Elastin was not extracted. Studies on the fibrillation of the extracted collagen in neutral solution at 25 degrees C or on the results of pepsin digestion in acidic solution at +4 degrees C showed that the tartaric acid-extracted collagen was in a nondenatured form, whereas that extracted by guanidinium Cl was largely denatured. Polyacrylamide gel electrophoresis (PAGE) indicated that most of the collagen was of type I and that many noncollagen proteins were present, mostly in the molecular weight range of 40 kDa. Bidimensional PAGE gave a reproducible pattern of these noncollagen proteins, showing that several additional proteins were present in tartaric acid extracts and not in guanidinium chloride extracts.


Asunto(s)
Colágeno/aislamiento & purificación , Tejido Conectivo/análisis , Proteínas/aislamiento & purificación , Animales , Electroforesis en Gel de Poliacrilamida , Guanidina , Guanidinas , Desnaturalización Proteica , Conejos , Tartratos
20.
Clin Physiol Biochem ; 3(5): 221-5, 1985.
Artículo en Inglés | MEDLINE | ID: mdl-3902319

RESUMEN

The effect of colchicine was studied in 51 hypertensive subjects with several other vascular risk factors. Colchicine was administered for 3-4 months in a daily dose of 1 mg per os. The treatment did not change the lipid content in the blood and in skin biopsies, and had no effect on systolic and diastolic blood pressure. On the contrary, colchicine treatment significantly improved the conjunctival biomicroscopy score, the duration of the dicrotic wave and the peripheral resistance index. The results show the improvement of the microcirculatory parameters (elasticity of arteries) without changes of serum and tissue lipid parameters in the patients treated with colchicine.


Asunto(s)
Arteriosclerosis/tratamiento farmacológico , Colchicina/uso terapéutico , Conjuntiva/patología , Hipertensión/tratamiento farmacológico , Adulto , Anciano , Apolipoproteínas/sangre , Arteriosclerosis/metabolismo , Arteriosclerosis/patología , Presión Sanguínea/efectos de los fármacos , Colesterol/metabolismo , Ensayos Clínicos como Asunto , Conjuntiva/efectos de los fármacos , Femenino , Humanos , Lípidos/sangre , Masculino , Persona de Mediana Edad , Piel/efectos de los fármacos , Piel/metabolismo
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