Characterization of a Gelatinase from Human Rheumatoid Synovial Fluid Cells

Kolkenbrock, Hansjörg; Ali, Haroon; Hecker-Kia, Adelheid; Buchlow, G.; Sørensen, Hilde Nebb; Hauer, R. W.; Ulbrich, Norbert

doi:10.1515/cclm.1991.29.8.499

Cited by 4 publications

(6 citation statements)

References 31 publications

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“…Several previous studies report that MMP-9 is unable to digest native collagen I [5,6,18,19,23]. In two of these [19,23], the precise assay conditions are not described and it is therefore difficult to compare these findings with the data reported here. Aimes and Quigley [5], Konttinen et al [6] and Murphy et al [18] performed assays at either 22 or 25°C and reported no digestion at these temperatures, in agreement with the findings of this study.…”

Section: Discussionmentioning

confidence: 54%

“…Several previous studies report that MMP‐9 is unable to digest native collagen I [5,6,18,19,23]. In two of these [19,23], the precise assay conditions are not described and it is therefore difficult to compare these findings with the data reported here. Aimes and Quigley [5], Konttinen et al .…”

Section: Discussionmentioning

confidence: 61%

“…A number of previous reports have investigated the ability of MMP-9 to degrade native collagen types I and III [5,6,[18][19][20][21][22][23] with disparate results. In this study, recombinant human MMP-9 was expressed in insect cells and the ability of enzyme purified from this source to digest native collagens I and III was evaluated.…”

Section: Discussionmentioning

confidence: 99%

“…To date, MMP‐9 has not been described as a collagenase. Several previous studies have investigated its ability to digest native collagen types I, II and III using enzyme from a variety of sources, both natural and recombinant [5,6,18–23]. Three of these demonstrated an inability to degrade soluble native collagen I at 22 or 25 °C [5,6,18]; a lack of digestion at 37 °C was additionally reported by Murphy et al .…”

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Activity of matrix metalloproteinase‐9 against native collagen types I and III

Bigg¹,

et al. 2007

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Collagens are the major structural proteins of connective tissues such as skin, bone, cartilage and tendon. Interstitial collagen types I, II and III are the most abundant, and the native triple helical structure of these molecules makes them highly resistant to proteolysis. However, collagenases of the matrix metalloproteinase (MMP) family [1] cleave native collagen types I, II and III at a specific site in all three chains of the triple helix, approximately three-quarters of the length from the N-terminus. The action of these collagenase enzymes is therefore critical for the initiation of collagenolysis. Once initiated, the cleaved helix unwinds at physiological temperatures and becomes susceptible to degradation by other, less-specific proteinases. MMP collagenases are active at neutral pH and play a highly important role in collagen degradation in vivo. The mammalian MMP collagenases currently include the 'classical' collagenases, MMP-1, and also the gelatinolytic enzyme, , and MMP-14 (MT1-MMP) [8], a member of the membrane-type subclass of MMPs.MMP-9 (also known as gelatinase B, 92 kDa gelatinase or 92 kDa type IV collagenase, EC 3.4.24.35) shares a close structural similarity with MMP-2 [9,10]. It was originally identified as a gelatinolytic enzyme produced by polymorphonuclear leukocytes [11] and subsequent studies have demonstrated secretion in the latent form (proMMP-9) by a variety of cell types. It has also been implicated in the pathogenesis of several human diseases, including arthritis [12][13][14][15]. Unlike other MMPs, MMP-9 and MMP-2 both contain three fibronectin type II repeats inserted into the catalytic Interstitial collagen types I, II and III are highly resistant to proteolytic attack, due to their triple helical structure, but can be cleaved by matrix metalloproteinase (MMP) collagenases at a specific site, approximately three-quarters of the length from the N-terminus of each chain. MMP-2 and -9 are closely related at the structural level, but MMP-2, and not MMP-9, has been previously described as a collagenase. This report investigates the ability of purified recombinant human MMP-9 produced in insect cells to degrade native collagen types I and III. Purified MMP-9 was able to cleave the soluble, monomeric forms of native collagen types I and III at 37°C and 25°C, respectively. Activity against collagens I and III was abolished by metalloproteinase inhibitors and was not present in the concentrated crude medium of mock-transfected cells, demonstrating that it was MMP-9-derived. Mutated, collagenase-resistant type I collagen was not digested by MMP-9, indicating that the three-quarters ⁄ one-quarter locus was the site of initial attack. Digestion of type III collagen generated a three-quarter fragment, as shown by comparison with MMP-1-mediated cleavage. These data demonstrate that MMP-9, like MMP-2, is able to cleave collagens I and III in their native form and in a manner that is characteristic of the unique collagenolytic activity of MMP collagenases.Abbreviations APMA, p-aminopheny...

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Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 99%

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Activity of matrix metalloproteinase‐9 against native collagen types I and III

Bigg¹,

et al. 2007

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“…The activator was much less active than trypsin in the proteolysis of casein and gelatin. However, although trypsin is a potent activator for polymorphonuclear leukocyte progelatinase (16), the stromelysin activator is about 30 times more efficient. The activator displays a similar efficiency in the activation of polymorphonuclear leukocyte collagenase, while the fibroblast M T 72 000 progelatinase is not a substrate for the activator.…”

Section: Discussionmentioning

confidence: 99%

A Trypsin Sensitive Stromelysin Isolated from Rheumatoid Synovial Fluid is an Activator for Matrix Metalloproteinases

Kolkenbrock¹,

Hecker-Kia²,

Orgel³

et al. 1993

Clinical Chemistry and Laboratory Medicine

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Summary:The processing of synovial fluids of patients suffering from rheumatoid arthritis led to the characterization of a neutral metalloproteinase with polymorphonuclear leukocyte progelatinase and polymorphonuclear leukocyte procollagenase activating properties. The activator exhibits a relative molecular mass of M t 27000 and is an active form of Stromelysin. Thus, it reacts specifically with antibodies raised against human Stromelysin, splits polymorphonuclear leukocyte progelatinase in a manner characteristic of Stromelysin, and is inhibited by EDTA as well as by a tissue inhibitor of metalloproteinases (TIMP-2).The activator shows a high specificity for the matrix metalloproteinases, polymorphonuclear leukocyte progelatinase and polymorphonuclear leukocyte procollagenase. It shows only weak hydrolysis of casein and gelatin, and it does not activate fibroblast Μ τ 72 000 progelatinase. Brief treatment with trypsin does not lead to a significant change in the activator's relative molecular mass, but induces a rapid loss of its activating activity for polymorphonuclear leukocyte progelatinase, while its proteolytic activity against the synthetic substrate, N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Z)-Arg, is increased about 3-fold. The same tryptic treatment does not affect the activator's proteolytic activity towards casein and gelatin. Introduction., . " ^ , .

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