Addendum to Partial Amino-Acid Sequence of Human PMN Leukocyte Procollagenase

Knauper,; Kramer, Steven J.; Reinke, Heinz; Tschesche, Harald

doi:10.1515/bchm3.1990.371.2.733

Cited by 15 publications

(9 citation statements)

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“…Considering recent data on multistep chromatography techniques for similar enzymes (e.g. [30]), the amounts of gelatinase produced by the neutrophils seem to be comparable to those of procollagenase, yet the two-step purification technology described here is much simpler and more convenient. Furthermore, the intact enzyme and its fragments could be separated by SDSjPAGE and sequenced after electroblotting to a ProblottTM membrane.…”

Section: Discussionmentioning

confidence: 87%

Purification and identification of 91‐kDa neutrophil gelatinase

Masure

Proost

Damme

et al. 1991

European Journal of Biochemistry

246

176

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Human neutrophils were found to release a 91 -kDa gelatinase that is serologically related to tumor-derived gelatinolytic enzymes, as evidenced by immunoprecipitation. In order to identify the neutrophil gelatinase, the activity in conditioned medium from human neutrophil suspensions was purified by affinity chromatography on a gelatin substrate. The 91-kDa active enzyme was further separated from other stainable protein bands by classical SDSjPAGE and blotting to a solid support. Amino-terminal sequence analysis of blotted proteins showed that the 91-kDa enzyme is a truncated form of tumor-derived 92-kDa gelatinase (type IV collagenase), lacking eight residues at the NH2-terminus. Sequence analysis of enzymatically inactive cleavage products of this neutrophil gelatinase demonstrated that the gelatin-binding part of the molecule is restricted to the amino-terminal third.Exocytosis of gelatinase-containing granules from neutrophils occurred spontaneously within 6 h after neutrophil plating. When the cells were triggered with the phorbol ester phorbol 12-myristate 13-acetate, a strong secretagogue, rapid gelatinase release was observed. When granulocytes were stimulated with the neutrophilactivating peptide interleukin-8, maximal exocytosis occurred within 1 h. The almost immediate release of neutrophil gelatinase after stimulation of the cells with a chemotactic factor might play a key role in remodeling of the extracellular matrix during granulocyte movement in response to chemotactic stimuli.Granulocytes, in particular neutrophils, play an important role in destroying pathogenic microorganisms as part of the aspecific immune response during acute inflammation. They are also involved in a variety of chronic inflammatory processes occurring in, for example, autoimmune diseases. Destruction and remodeling of connective tissues in acute and chronic inflammatory disorders is regulated by cytokines and mediated through the combined effect of molecules such as reactive oxidants and various proteolytic enzymes. Some cytokines, e. g. interleukin-I (IL-I), have been reported to induce proteinase secretion in the inflamed tissue directly, whereas others such as locally produced interleukin-8 (IL-8) attract leukocytes which can then release an array of proteolytic enzymes [l]. Among these are leukocytic serine proteinases, e.g. elastase and plasminogen activators and the metalloproteinases collagenase and gelatinase. These enzymes are actively synthesized and secreted or released from preformed granules by the infiltrating leukocytes [2 -41.Human polymorphonuclear leukocytes have been shown to secrete a specific type of collagenase not found in other cell types. This fully characterized protein has a molecular mass of 75 kDa and degrades native collagen types I, I1 and 111 [5 -71. A less well characterized gelatinase of molecular mass 92 kDa has also been detected in polymorphonuclear leukocytes [8, 91. This enzyme degrades denatured collagens (gelatins) and types IV and V collagen. Both enzymes have been shown to be stor...

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Section: Discussionmentioning

confidence: 87%

Purification and identification of 91‐kDa neutrophil gelatinase

Masure

Proost

Damme

et al. 1991

European Journal of Biochemistry

246

176

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“…The antibody used in IFMA identifies neutrophilic and fibroblast‐type MMP‐8 isotypes and in particular their active forms (Hanemaaijer et al 1997, Sorsa et al 2010). Unlike IFMA, the ELISA method detects all forms of MMP‐8, as the antibodies have been produced against full‐size MMP‐8 (Knäuper et al 1990). With regard to our latest study (Sorsa et al 2010) on the detection of MMP‐8 in GCF with IFMA antibody, it was shown that the major bands in Western blots were 55 kDa MMP‐8 species in the periodontitis group.…”

Section: Discussionmentioning

confidence: 99%

Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced periodontitis

Gürsoy

Könönen

Pradhan-Palikhe

et al. 2010

J Clinic Periodontology

179

227

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“…Amino acid sequencing revealed a lack of signal for the Asn 98 residue, thus it can be deduced that the glycosylation site N 98 LT carries N-linked sugars. This glycosylation site is conserved between collagenase-3, neutrophil collagenase (Knä uper et al, 1990b), and gelatinase-B and is occupied in all three enzymes. The role of the high levels of glycosylation observed for these three enzymes is not quite clear to date.…”

Section: Discussionmentioning

confidence: 99%

“…The interaction of the collagenases with TIMPs is mainly regulated by the catalytic domain , but C-terminal domain interactions increase the association rates of complex formation. Biochemical studies on fibroblast and neutrophil collagenases describing their activation mechanism, substrate specificity, and inhibitor interaction in relation to their domain organization are well advanced (Murphy et al, 1987Clark and Cawston, 1989;Hirose et al, 1993;Sanchez-Lopez et al, 1993;Knä uper et al, 1990aKnä uper et al, , 1990bKnä uper et al, , 1993aKnä uper et al, , 1993b, but there are currently no data available regarding the activation * This work was supported in part by the Arthritis and Rheumatism Council, United Kingdom, by a Wellcome Trust Travelling Fellowship (to V. K.) and by Comision Interministerial de Ciencia y Tecnologia Spain Project . The costs of publication of this article were defrayed in part by the payment of page charges.…”

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confidence: 99%

Biochemical Characterization of Human Collagenase-3

Knäuper¹,

López-Otı́n

Smith

et al. 1996

Journal of Biological Chemistry

Self Cite

823

683

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The cDNA of a novel matrix metalloproteinase, collagenase-3 (MMP-13) has been isolated from a breast tumor library (Freije, J. M. P., Diez-Itza, I., Balbin, M., Sanchez, L. M., Blasco, R., Tolivia, J., and Ló pez-Otin, C. (1994) J. Biol. Chem. 269, 16766 -16773), and a potential role in tumor progression has been proposed for this enzyme. In order to establish the possible role of collagenase-3 in connective tissue turnover, we have expressed and purified recombinant human procollagenase-3 and characterized the enzyme biochemically. The purified procollagenase-3 was shown to be glycosylated and displayed a M r of 60,000, the N-terminal sequence being LPLPSGGD, which is consistent with the cDNA-predicted sequence. The proenzyme was activated by p-aminophenylmercuric acetate or stromelysin, yielding an intermediate form of M r 50,000, which displayed the N-terminal sequence L 58 EVTGK. Further processing resulted in cleavage of the Glu 84 -Tyr 85 peptide bond to the final active enzyme (M r 48,000). Trypsin activation of procollagenase-3 also generated a Tyr 85 N terminus, but it was evident that the C-terminal domain was rapidly lost, and hence the collagenolytic activity diminished. Analysis of the substrate specificity of collagenase-3 revealed that soluble type II collagen was preferentially hydrolyzed, while the enzyme was 5 or 6 times less efficient at cleaving type I or III collagen. Fibrillar type I collagen was cleaved with comparable efficiency to the fibroblast and neutrophil collagenases (MMP-1 and MMP-8), respectively. Unlike these collagenases, gelatin and the peptide substrates Mca-ProLeu-Gly-Leu-Dpa-Ala-Arg-NH 2 and Mca-Pro-Cha-GlyNva-His-Ala-Dpa-NH 2 were efficiently hydrolyzed as well, as would be predicted from the similarities between the active site sequence of collagenase-3 (MMP-13) and the gelatinases A and B. Active collagenase-3 was inhibited in a 1:1 stoichiometric fashion by the tissue inhibitors of metalloproteinases, TIMP-1, TIMP-2, and TIMP-3. These results suggest that in vivo collagenase-3 could play a significant role in the turnover of connective tissue matrix constituents.

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Addendum to Partial Amino-Acid Sequence of Human PMN Leukocyte Procollagenase

Cited by 15 publications

References 0 publications

Purification and identification of 91‐kDa neutrophil gelatinase

Purification and identification of 91‐kDa neutrophil gelatinase

Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced periodontitis

Biochemical Characterization of Human Collagenase-3

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