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2.
J Ayub Med Coll Abbottabad ; 29(2): 355-357, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28718266

RESUMO

Prolidase deficiency is a rare autosomal recessive disorder characterized by recurrent and nonhealing skin ulcers along with facial dysmorphism and mental retardation. We report a 13-year-old girl who has clinical manifestation of Proliodase deficiency. It is a very rare disorder and no such case has been reported so far from Pakistan.


Assuntos
Dipeptidases/metabolismo , Deficiência de Prolidase/diagnóstico , Administração Tópica , Adolescente , Feminino , Glucocorticoides/uso terapêutico , Glicina/administração & dosagem , Humanos , Plasmaferese , Deficiência de Prolidase/metabolismo , Deficiência de Prolidase/terapia , Prolina/administração & dosagem
3.
Eur J Paediatr Dent ; 15(2 Suppl): 224-8, 2014 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-25101509

RESUMO

BACKGROUND: Prolidase Deficiency (PD) is a rare hereditary disease consisting in developmental delay, mental retardation, facial dysmorphism, splenomegaly, recurrent pulmonary infections and skin lesions. CASE REPORT: The present study reports a case of PD treated in the Paediatric Section of the Department of Dentistry and Surgery at the University of Bari. A special diagnostic and clinical approach to the patient was useful to improve his quality of life and identify some new aspects of this systemic disease. In particular, clinical features never described before are reported: low hair line, decreased osteotendinous reflexes, long upper lip, microrhinia, dentoskeletal Class III, dental age (Proffit) older than chronological age, fusion of 2nd and 3rd cervical vertebrae, incomplete atlanto-occipital fusion.


Assuntos
Face , Deficiência de Prolidase/complicações , Anormalidades Dentárias/etiologia , Cefalometria , Criança , Humanos , Masculino , Deficiência de Prolidase/terapia , Radiografia Panorâmica
4.
PLoS One ; 8(3): e58792, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23516557

RESUMO

Prolidase is the only human enzyme responsible for the digestion of iminodipeptides containing proline or hydroxyproline at their C-terminal end, being a key player in extracellular matrix remodeling. Prolidase deficiency (PD) is an intractable loss of function disease, characterized by mutations in the prolidase gene. The exact causes of activity impairment in mutant prolidase are still unknown. We generated three recombinant prolidase forms, hRecProl-231delY, hRecProl-E412K and hRecProl-G448R, reproducing three mutations identified in homozygous PD patients. The enzymes showed very low catalytic efficiency, thermal instability and changes in protein conformation. No variation of Mn(II) cofactor affinity was detected for hRecProl-E412K; a compromised ability to bind the cofactor was found in hRecProl-231delY and Mn(II) was totally absent in hRecProl-G448R. Furthermore, local structure perturbations for all three mutants were predicted by in silico analysis. Our biochemical investigation of the three causative alleles identified in perturbed folding/instability, and in consequent partial prolidase degradation, the main reasons for enzyme inactivity. Based on the above considerations we were able to rescue part of the prolidase activity in patients' fibroblasts through the induction of Heath Shock Proteins expression, hinting at new promising avenues for PD treatment.


Assuntos
Dipeptidases/química , Dipeptidases/metabolismo , Mutação , Deficiência de Prolidase/enzimologia , Deficiência de Prolidase/genética , Coenzimas/metabolismo , Biologia Computacional , Dipeptidases/genética , Estabilidade Enzimática , Fibroblastos/enzimologia , Proteínas de Choque Térmico/metabolismo , Humanos , Cinética , Manganês/metabolismo , Modelos Moleculares , Deficiência de Prolidase/patologia , Deficiência de Prolidase/terapia , Multimerização Proteica , Estrutura Quaternária de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Temperatura
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