The structure and assembly of procollagen – a review

Börnstein, Paul

doi:10.1002/jss.400020206

Cited by 12 publications

(1 citation statement)

References 75 publications

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“…This process is known as zymogen activation, a term which initially was applied to the activation of precursors of proteolytic enzymes such as trypsinogen, chymotrypsinogen, or procarboxypeptidase (1). It is now apparent that the same type of reaction is involved in a great variety of biological processes, such as blood coagulation, fibrinolysis, complement reaction, hormone production, development, differentiation, and supramolecular assembly, all of which involve zymogen activation in one or more steps (2)(3)(4)(5)(6)(7)(8)(9). In the present article, we shall attempt to show that activation by limited proteolysis is indeed an important control element which can initiate new physiological functions or regulate preexistent ones.…”

mentioning

confidence: 99%

Role of proteolytic enzymes in biological regulation (a review).

Neurath¹,

Walsh²

1976

Proc. Natl. Acad. Sci. U.S.A.

386

204

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Many enzymes, hormones, and other physiologically active proteins are synthesized as inactive precursors (zymogens) that are subsequently converted to the active form by the selective enzymatic cleavage (limited proteolysis) of peptide bonds. The ultimate agency of activating enzymatic function is limited proteolysis, either in a single activation step or in a consecutive series (cascade). The specificity of each activation reaction is determined by the complementarity of the zymogen substrate and the active site of the attacking protease. The sequence of consecutive activation reactions is regulated by the specificity of each enzyme, whereas the degree of amplification of the initial stimulus is determined by the efficiency of each activating step.Zymogen activation produces a prompt and irreversible response to a physiological stimulus, and is capable of initiating new physiological functions. Typical examples are the processes of blood coagulation, fibrinolysis, complement activation, hormone production, metamorphosis, rtilization, supramolecular assembly, and digestion. The zymogens of the pancreatic serine proteases, in particular, have served as models for detailed studies of the nature of the molecular changes that are involved in the dramatic increase in enzymatic activity that ensues upon limited proteolysis of the zymogen. In recent years, it has become evident that many proteins are synthesized as inactive precursors or zymogens and that these are subsequently converted to physiologically active forms by the selective enzymatic cleavage of peptide bonds. This process is known as zymogen activation, a term which initially was applied to the activation of precursors of proteolytic enzymes such as trypsinogen, chymotrypsinogen, or procarboxypeptidase (1). It is now apparent that the same type of reaction is involved in a great variety of biological processes, such as blood coagulation, fibrinolysis, complement reaction, hormone production, development, differentiation, and supramolecular assembly, all of which involve zymogen activation in one or more steps (2-9). In the present article, we shall attempt to show that activation by limited proteolysis is indeed an important control element which can initiate new physiological functions or regulate preexistent ones.Virtually all zymogen activation reactions require the en- The position of zymogen activation in the overall scheme of physiological control processes is diagrammatically shown in Fig.

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mentioning

confidence: 99%

Role of proteolytic enzymes in biological regulation (a review).

Neurath¹,

Walsh²

1976

Proc. Natl. Acad. Sci. U.S.A.

386

204

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Procollagen Biosynthesis in Mammalian Cells

Tasab

Bulleid

2008

Protein Science Encyclopedia

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Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2 The sections in this article are Introduction Variety and Complexity of Collagen Proteins Fibrillar Procollagen Expression of Fibrillar Collagens The Procollagen Biosynthetic Process: An Overview Disulfide Bonding in Procollagen Assembly The Influence of Primary Amino Acid Sequence on Intracellular Procollagen Folding Chain Recognition and Type‐specific Assembly Assembly of Multi‐subunit Proteins Coordination of Type‐specific Procollagen Assembly and Chain Selection Hypervariable Motifs: Components of a Recognition Mechanism That Distinguishes Between Procollagen Chains? Modeling the C ‐propeptide Chain Association Posttranslational Modifications That Affect Procollagen Folding Hydroxylation and Triple‐helix Stability Procollagen Chaperones Prolyl 4‐Hydroxylase Protein Disulfide Isomerase Hsp 47 PPI and Bi P Analysis of Procollagen Folding

show abstract

Procollagen Biosynthesis in Mammalian Cells

Tasab¹,

Bulleid²

2005

Protein Folding Handbook

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The structure and assembly of procollagen – a review

Cited by 12 publications

References 75 publications

Role of proteolytic enzymes in biological regulation (a review).

Role of proteolytic enzymes in biological regulation (a review).

Procollagen Biosynthesis in Mammalian Cells

Procollagen Biosynthesis in Mammalian Cells

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