[8] Catabolism and turnover of collagens: Collagenases

Birkedal‐Hansen, Henning

doi:10.1016/0076-6879(87)44177-3

Cited by 137 publications

(106 citation statements)

References 57 publications

Supporting

Mentioning

104

Contrasting

Order By: Relevance

“…Comparing the collagenases of bacteria and vertebrates, the former show broad substrate specificity and degrade both native and denatured collagens (Peterkofsky, 1982), while the latter preferentially cleave the native form at a specific site and other proteases are necessary for complete degradation (Birkeday-Hansen, 1987). The destructive power of bacterial collagenase has been widely used for the disintegration of connective tissue, separation of tissue culture cells (Wolters et al, 1995), selective cleavage of gene products in biotechnology (Sassenfeld, 1990), improving the tenderness of meat (Miller et al, 1989) and also for clinical therapy to eliminate necrotic tissue from burns, ulcers and decubitus (Ohmi et al, 1989;Sank et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Expression and characterization of the prtV gene encoding a collagenase from Vibrio parahaemolyticus in Escherichia coli

Yu¹,

Lee²

1999

Microbiology

View full text Add to dashboard Cite

The prtV gene, encoding a collagenase of Vibrio parahaemolyticus, was expressed in Escherichia coli and purified by affinity chromatography. The transformant E. coli BL2l (DE3)(pPRT2) secreted the recombinant Prtv, and the highest enzyme activity was detected in the culture supernatant after 5 h IPTG induction. The molecular mass o f purified PrtV was 62 kDa as determined by gel filtration, which was similar to that obtained by SDS-PAGE (64 kDa). This suggested that PrtV was a monomer protein having no subunit structure. The isoelectric point o f PrtV was 852. In addition, PrtV contained a 27 amino acid signal peptide, and the amino acid composition of the PrtV showed satisfactory agreement with that predicted from the DNA sequence. The optimum temperature and pH of PrtV were 40 OC and pH 7.5, respectively. The activity of PrtV was inhibited by chelators such as EDTA, EGTA and 1,lOphenanthroline; however, its activity was restored by the addition of various metal ions (Co2+, Mn2+, Ca2+, Cu2+, Ni2+ and Zn2+), indicating that PrtV is a metalloprotease. PrtV degraded both type I collagen and synthetic substrate FALGPA well, showing that PrtV is indeed a collagenase.

show abstract

Section: Discussionmentioning

confidence: 99%

Expression and characterization of the prtV gene encoding a collagenase from Vibrio parahaemolyticus in Escherichia coli

Yu¹,

Lee²

1999

Microbiology

View full text Add to dashboard Cite

show abstract

“…Several other MMPs also share this property (Birkedal-Hansen, 1995). Collagenase exerts its action on interstitial collagens (types 1, 11, 111) by an initial single scission of a Gly775 -111776 or Gly775 -Leu776 of the a-chains, to render products of 3/4 and 1/4 of the length of the collagen molecule (Birkedal-Hansen, 1987). it has been suggested that the collagenase-sensitive region of the collagen molecule represents a locus of minor resistance that more readily unfolds and relaxes its triple helical structure than other parts of the molecule (Fields et al, 1987).…”

Section: (G) Influence Of Il-i On Collagen Synthesismentioning

confidence: 99%

Factors Affecting IL-1-Mediated Collagen Metabolism By Fibroblasts and the Pathogenesis of Periodontal Disease: A Review of the Literature

Havemose-Poulsen

Holmstrup

1997

Critical Reviews in Oral Biology & Medicine

View full text Add to dashboard Cite

Fibroblasts have been studied extensively for their contribution to connective tissue destruction in diseases where the metabolism of extracellular matrix components plays an essential part in their pathogenesis. A considerable dissolution, especially of collagen fibrils, is a well-known characteristic of the periodontal ligament and the gingival connective tissue in microbial-induced periodontal disease. Fibroblasts, responsible for the assembly of the extracellular matrix, are capable of responding directly to oral microbial challenges or indirectly, following activation of the host immune response, and can alter the composition of connective tissue in several ways: synthesis of inflammatory mediators, their receptors and antagonists; fibroblast proliferation; collagen synthesis; phagocytosis of collagen fibrils; and synthesis of proteolytic enzymes, including matrix metalloproteinases and their corresponding inhibitors. The contributions of these cellular fibroblastic properties to the pathogenesis of periodontal disease are reviewed in the context of the cytokine, interleukin-l, as the inflammatory regulator.

show abstract

“…The MMPs are a family of zinc-dependent proteases [9]. These proteases were originally recognized for their ability to degrade a variety of extracellular matrix (ECM) components.…”

Section: Proteases Matrix Metalloproteinases (Mmps)mentioning

confidence: 99%

Proteases as modulators of tumor–stromal interaction: Primary tumors to bone metastases

Wilson

Singh

2008

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

View full text Add to dashboard Cite

SummaryAs cells undergo oncogenic transformation and as transformed cells arrive at metastatic sites, a complex interplay occurs with the surrounding stroma. This dialogue between tumor and stroma ultimately dictates the success of the tumor cells in the given microenvironment. As a result, understanding the molecular mechanisms at work is important for developing new therapeutic modalities. Proteases are major players in the interaction between tumor and stroma. This review will focus on the role of proteases in modulating tumor-stromal interactions of both primary breast and prostate tumors as well as at bone metastatic sites in a way that favors tumor growth.

show abstract

[8] Catabolism and turnover of collagens: Collagenases

Cited by 137 publications

References 57 publications

Expression and characterization of the prtV gene encoding a collagenase from Vibrio parahaemolyticus in Escherichia coli

Expression and characterization of the prtV gene encoding a collagenase from Vibrio parahaemolyticus in Escherichia coli

Factors Affecting IL-1-Mediated Collagen Metabolism By Fibroblasts and the Pathogenesis of Periodontal Disease: A Review of the Literature

Proteases as modulators of tumor–stromal interaction: Primary tumors to bone metastases

Contact Info

Product

Resources

About