Proparathyroid Hormone Is Preferentially Cleaved to Parathyroid Hormone by the Prohormone Convertase Furin (Q55953364)

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Hugh P. J. Bennett

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Bernard F. Gibbs

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Claude Lazure

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Robert Day

Journal of Biological Chemistry

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language of work or name

English

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publication date

21 April 1995

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published in

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volume

270

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issue

16

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page(s)

9517-9525

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cites work

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Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes

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cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases

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Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2.

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Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans

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Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats

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Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15

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Testicular expression of PC4 in the rat: molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase

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Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4

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PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues

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Isolation and analysis of human parathyrin in parathyroid tissue and plasma Use of reversed-phase liquid chromatography

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Synthesis and characterization of extended and deleted recombinant analogues of parathyroid hormone-(1-84): correlation of peptide structure with function.

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Mammalian subtilisins: the long-sought dibasic processing endoproteases

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Electron microscopic immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic beta-cells

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Calcium-Dependent Intracellular Degradation of Parathyroid Hormone: A Possible Mechanism for the Regulation of Hormone Stores12

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Proteolytic processing of chromogranin A in purified insulin granules. Formation of a 20 kDa N-terminal fragment (betagranin) by the concerted action of a Ca2+-dependent endopeptidase and carboxypeptidase H (EC 3.4.17.10)

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