Regulation of Proteolytic Activity in Tissues

Twining, Sally S.

doi:10.3109/10409239409083484

Cited by 100 publications

(64 citation statements)

References 330 publications

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“…Examples can be found in digestion, blood coagulation and fibrinolysis, processing of preproproteins such as collagen, immune function, development, and apoptosis (reviewed in Twining, 1994). Not surprisingly, peptidase genes are found in the genomes of all cellular organisms (and several types of virus), and there are arrays of proteolytic enzymes distributed in cellular and tissue compartments.…”

Section: (A) Overview Of Peptidasesmentioning

confidence: 99%

“…This degradation is mediated in part by a diverse collection of peptidases. In the neutrophil, these include the azurophil granule serine peptidases elastase, cathepsin G, and proteinase 3, and the aspartate peptidase cathepsin D, and the metallopeptidases collagenase (MMP8) and gelatinase in other granules (Sandborg and Smolen, 1988;Twining, 1994). The serine peptidase concentration in neutrophils is a considerable 3 M (Travis et al, 1994), and in a healthy individual an estimated 2 g of elastase and 1.5 g of cathepsin G are released each day (Travis and Bangalore, 1993).…”

Section: (3):238-275 (2002)mentioning

confidence: 99%

“…Several mechanisms are used to regulate peptidase activity, in addition to transcriptional and post-transcriptional controls (Twining, 1994;Chapman et al, 1997). Most enzymes are synthesized as inactive zymogens that must be activated by proteolytic cleavage.…”

Section: (C) Regulation Of Cps and Other Peptidasesmentioning

confidence: 99%

“…Tissues and fluids contain a large number of protein peptidase inhibitors that inactivate serine peptidases (the serine peptidase inhibitors, or serpins; and the Kazal, Kunitz, and leukoproteinase types of inhibitors), CPs (members of the cystatin superfamily), and metallopeptidases (e.g., the tissue inhibitors, TIMPs) (reviewed in Travis and Salvesen, 1983;Twining, 1994;Roberts et al, 1995). There are no known specific inhibitors of aspartate peptidases, but it is generally assumed that ␣ 2 -macroglobulin (a broad-spectrum peptidase inhibitor) serves this purpose.…”

Section: (Vi) the Proteolytic Cascade: Interactions Between Enzymes Amentioning

confidence: 99%

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Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

158

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Cysteine peptidases (CPs) are phylogenetically ubiquitous enzymes that can be classified into clans of evolutionarily independent proteins based on the structural organization of the active site. In mammals, two of the major clans represented in the genome are: the CA clan, whose members share a structure and evolutionary history with papain; and the CD clan, which includes the legumains and caspases. This review focuses on the properties of these enzymes, with an emphasis on their potential roles in the oral cavity. The human genome encodes at least (but possibly no more than) 11 distinct enzymes, called cathepsins, that are members of the papain family C1A. Ten of these are present in rodents, which also carry additional genes encoding other cathepsins and cathepsin-like proteins. Human cathepsins are best known from the ubiquitously expressed lysosomal cathepsins B, H, and L, and dipeptidyl peptidase I (DPP I), which until recently were considered to mediate primarily "housekeeping" functions in the cell. However, mutations in DPP I have now been shown to underlie Papillon-Lefèvre syndrome and pre-pubertal periodontitis. Other cathepsins are involved in tissue-specific functions such as bone remodeling, but relatively little is known about the functions of several recently discovered enzymes. Collectively, CPs participate in multiple host systems that are active in health and in disease. They are involved in tissue remodeling and turnover of the extracellular matrix, immune system function, and modulation and alteration of cell function. Intracellularly, CPs function in diverse processes including normal protein turnover, antigen and proprotein processing, and apoptosis. Extracellularly, they can contribute directly to the degradation of foreign proteins and the extracellular matrix. However, CPs can also participate in proteolytic cascades that amplify the degradative capacity, potentially leading to pathological damage, and facilitating the penetration of tissues by cancer cells. We know relatively little regarding the role of human CPs in the oral cavity in health or disease. Most studies to date have focused on the potential use of the lysosomal enzymes as markers for periodontal disease activity. Human saliva contains high levels of cystatins, which are potent CP inhibitors. Although these proteins are presumed to serve a protective function, their in vivo targets are unknown, and it remains to be discovered whether they serve to control any human CP activity.

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Section: (A) Overview Of Peptidasesmentioning

confidence: 99%

Section: (3):238-275 (2002)mentioning

confidence: 99%

Section: (C) Regulation Of Cps and Other Peptidasesmentioning

confidence: 99%

Section: (Vi) the Proteolytic Cascade: Interactions Between Enzymes Amentioning

confidence: 99%

See 2 more Smart Citations

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

158

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“…Awal ketidak seimbangan antar MMP-1 dan jaringan penghambat metalloproteinase 1/ Tissue inhibitor of matrix metalloproteinase (TIMP-1) bisa meningkatkan penuaan (19). MMP-1 diproduksi oleh keratinosites epidermal dan fibroblasts dermal sebagai respon atas berbagai stimuli, sepertinya memainkan peranan penting dalam mengubah bentuk lapisan dermis (20). Beberapa MMP diproduksi selama penyembuhan luka, seperti MMP-3 di perbaikan lapisan epidermis (21).…”

Section: Diskusiunclassified

EFEK EKSTRAK BUAH TOMAT (Licopersicum pyriforme) TERHADAP EKSP KOLAGEN TIPE 1, MMP-1 DAN MMP-3 PADA PENUAAN KULIT

Wahyono

2013

JKB

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Synthetic inhibitor of matrix metalloproteinases (batimastat) reduces prostate cancer growth in an orthotopic rat model

Lein

Jung

et al. 2000

Prostate

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Regulation of Proteolytic Activity in Tissues

Cited by 100 publications

References 330 publications

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

EFEK EKSTRAK BUAH TOMAT (Licopersicum pyriforme) TERHADAP EKSP KOLAGEN TIPE 1, MMP-1 DAN MMP-3 PADA PENUAAN KULIT

Synthetic inhibitor of matrix metalloproteinases (batimastat) reduces prostate cancer growth in an orthotopic rat model

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