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1.
World J Clin Cases ; 10(11): 3609-3614, 2022 Apr 16.
Artículo en Inglés | MEDLINE | ID: mdl-35582057

RESUMEN

BACKGROUND: The recognized pattern of cervical lymph node metastasis (CLNM) of papillary thyroid carcinoma involves a stepwise route. Contralateral lymph node skip metastasis is very rare. In addition, the patient in our case report also suffered from a breast carcinoma accompanied by left supraclavicular lymphadenopathy, which made it difficult to distinguish the origin of the CLNM. Based on this case, we recommended that more detailed physical and imaging examinations are needed for patients with uncommon cervical lymphatic metastasis of primary cancer. CASE SUMMARY: A 53-year-old women was admitted to the hospital for a neck mass in the left cervical region that had existed for 2 mo. The neck mass was suspected to be an enlarged lateral LN originating from papillary thyroid microcarcinoma of the contralateral thyroid lobe, according to ultrasound and ultrasound-guided fine needle aspiration biopsy. The patient underwent total thyroidectomy and radical cervical LN dissection. Postoperative pathology confirmed the diagnosis of papillary thyroid microcarcinoma with contralateral lymphatic skip metastasis. Unfortunately, a breast cancer was discovered 4 mo later, which was accompanied by ipsilateral supraclavicular LN metastasis. She accepted neoadjuvant chemotherapy and subsequent left modified radical mastectomy for treatment. The patient is currently receiving postoperative radiotherapy, and no local recurrence was observed in the 6-mo follow-up after surgery. CONCLUSION: We present a rare case of papillary thyroid microcarcinoma with contralateral lymphatic skip metastasis and breast cancer with supraclavicular lymphatic metastasis.

2.
DNA Seq ; 17(1): 1-7, 2006 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-16753811

RESUMEN

Deficiency of human glycerate kinase leads to D-glycerate acidemia/D-glyceric aciduria. Through PCR cloning assisted by in silico approach, we isolated the human glycerate kinase genes--Glycerate Kinase 1 (GLYCTK1) and its alternatively splicing variant--Glycerate Kinase 2 (GLYCTK2), which might be associated with D-glycerate acidemia/D-glyceric aciduria. The locus of GLYCTK gene is mapped to 3p21. PCR amplification in seventeen human tissue cDNAs revealed that both GLYCTK1 and GLYCTK2 are expressed widely almost in all these tissues. The expression of mouse Glyctk in various tissues was demonstrated by in situ hybridization. Both GLYCTK1 and GLYCTK2 proteins are localized in cytosol, and GLYCTK2 proteins are specifically localized in mitochondria. Present results revealed the characteristic expression pattern of murine Glyctk in neural system, skeleton muscle, supporting that glycerate kinase is implicated in D-glycerate acidemia/D-glyceric aciduria.


Asunto(s)
Ácidos Glicéricos/sangre , Fosfotransferasas (Aceptor de Grupo Alcohol)/genética , Isoformas de Proteínas/genética , Empalme Alternativo , Animales , Secuencia de Bases , Células COS , Chlorocebus aethiops , ADN Complementario/aislamiento & purificación , Variación Genética , Humanos , Hibridación in Situ , Hibridación Fluorescente in Situ , Ratones , Datos de Secuencia Molecular , Fosfotransferasas (Aceptor de Grupo Alcohol)/deficiencia , Proteínas Recombinantes de Fusión/análisis , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Distribución Tisular/genética
3.
Biotechnol Lett ; 28(17): 1327-33, 2006 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-16802092

RESUMEN

Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.


Asunto(s)
Proteínas Portadoras/genética , Proteínas Recombinantes/biosíntesis , Secuencia de Aminoácidos , Secuencia de Bases , Encéfalo/metabolismo , Proteínas Portadoras/biosíntesis , Proteínas Portadoras/química , Mapeo Cromosómico , Clonación Molecular , Células HeLa , Humanos , Datos de Secuencia Molecular , ARN Mensajero/análisis
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