Association of the rs6235 variant in the proprotein convertase subtilisin/kexin type 1 (PCSK1) gene with obesity and related traits in a Taiwanese population

Gene ◽  
2014 ◽  
Vol 533 (1) ◽  
pp. 32-37 ◽  
Author(s):  
Tun-Jen Hsiao ◽  
Yuchi Hwang ◽  
Hua-Mei Chang ◽  
Eugene Lin
Keyword(s):  
Proprotein Convertase ◽  
Taiwanese Population ◽  
Pcsk1 Gene

PCSK9 (proprotein convertase subtilisin/kexin type 9) in a patients with type 1 diabetes mellitus. Correlation with metabolic control and lipid metabolism

2018 ◽  
Vol 275 ◽  
pp. e250
Author(s):  
A.R. Guerra ruiz ◽  
B.A. Lavin Gomez ◽  
L. Ramos Ramos ◽  
J.L. Hernandez Hernandez ◽  
C. García Ibarbia ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 1 Diabetes ◽  
Lipid Metabolism ◽  
Type 1 Diabetes Mellitus ◽  
Metabolic Control ◽  
Proprotein Convertase

scholarly journals PCSK1 (proprotein convertase subtilisin/kexin type 1)

2018 ◽  
Author(s):  
Béatrice Demoures ◽  
Géraldine Siegfried ◽  
Abdel-Majid Khatib
Keyword(s):  
Proprotein Convertase

scholarly journals A Novel Familial Mutation in the PCSK1 Gene That Alters the Oxyanion Hole Residue of Proprotein Convertase 1/3 and Impairs Its Enzymatic Activity

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e108878 ◽  
Author(s):  
Michael Wilschanski ◽  
Montaser Abbasi ◽  
Elias Blanco ◽  
Iris Lindberg ◽  
Michael Yourshaw ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Proprotein Convertase ◽  
Oxyanion Hole ◽  
Pcsk1 Gene

scholarly journals Enteroendocrine Dysfunction in Two Saudi Sisters

2021 ◽  
pp. 290-295
Author(s):  
Amna Basheer M. Ahmed ◽  
Badr M. Rasheed Alsaleem
Keyword(s):  
Early Diagnosis ◽  
Effective Treatment ◽  
Early Onset ◽  
Autosomal Recessive ◽  
Autosomal Recessive Disorder ◽  
Proprotein Convertase ◽  
Whole Exome ◽  
Osmotic Diarrhea ◽  
Symptoms And Signs

Proprotein convertase (PC) deficiency is a rare autosomal recessive disorder caused by mutations in proprotein convertase subtilisin/kexin type 1 (PCSK1). It is characterized by severe malabsorptive early-onset diarrhea, obesity, and systemic endocrinopathies. Only few cases have been reported in the literature; we have add two female sisters with some difference in clinical progress. Herein, we describe two sisters with congenital osmotic diarrhea diagnosed with PC1/3 deficiency, causing malabsorptive diarrhea and enteroendocrine dysfunction, who presented with chronic enteropathy with hypernatremia but with different expressivity. PC1/3 deficiency presents with symptoms and signs that mimic glucose-galactose malabsorption. Because of the clinical paucity and heterogeneity of congenital enteropathies, whole-exome sequencing may be of great help towards early diagnosis and effective treatment.

scholarly journals Regulation of Membrane Type-1 Matrix Metalloproteinase Activation by Proprotein Convertases

2000 ◽  
Vol 11 (7) ◽  
pp. 2387-2401 ◽  
Author(s):  
Ikuo Yana ◽  
Stephen J. Weiss
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinase ◽  
Catalytic Domain ◽  
Extracellular Matrix Remodeling ◽  
Matrix Remodeling ◽  
Proprotein Convertase ◽  
Proprotein Convertases ◽  
Recognition Motifs ◽  
Membrane Type

Membrane type-1 matrix metalloproteinase (MT1-MMP) is the prototypical member of a subgroup of membrane-anchored proteinases that belong to the matrix metalloproteinase family. Although synthesized as a zymogen, MT1-MMP plays an essential role in extracellular matrix remodeling after an undefined process that unmasks its catalytic domain. We now report the existence of a proprotein convertase–MT1-MMP axis that regulates the processing and functional activity of the metalloproteinase. Two sets of basic motifs in the propeptide region of MT1-MMP are identified that potentially can be recognized by the proprotein convertase family of subtilisin-like proteases. Processing of proMT1-MMP as well as the expression of its proteolytic activity were blocked by mutating these recognition motifs or by inhibiting the proprotein convertases furin and PC6 with the serpin-based inhibitor α1 antitrypsin Portland. Furthermore, both furin-dependent and furin-independent MT1-MMP processing pathways are identified that require tethering of the metalloproteinase to the cell surface. These findings demonstrate the existence of a proprotein convertase–MT1-MMP axis that can regulate extracellular matrix remodeling.

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