Identification of a splice variant of neutrophil collagenase (MMP‐8)

Hu, S; Klein, Melissa; Carozza, M.A.; Rediske, John; Peppard, Jane; Qi, Jian-Shen

doi:10.1016/s0014-5793(98)01654-8

Cited by 14 publications

(8 citation statements)

References 16 publications

(16 reference statements)

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“…Unlike the secretion of gelatinases by plasma cells17, the detected inducible increases in MMP‐8 and MMP‐13 mRNA and proteins were observed inside rather than outside cultured plasma cells, suggesting that they may represent splice variants of these MMPs, as recently shown for MMP‐834. The splice variants may be released into the extracellular milieu upon cell death or apoptosis34.…”

Section: Discussionmentioning

confidence: 77%

Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions

et al. 2001

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Matrix metalloproteinases (MMPs) collectively degrade extracellular matrix and basement membrane proteins in chronic inflammation and bone-destructive lesions. This study examined the ability of immunoglobulin-producing plasma cells, typically present in sites of chronic inflammation, to express collagenases (MMP-8 and -13) in vivo and in vitro. Phorbol-12-myristate-13-acetate, interleukin-6, and tumour necrosis factor-alpha and heparin with the tumour promoter or cytokines potently enhanced (up to nine-fold) MMP-8 and -13 expression by the RPMI 8226 myeloma cell line, as evidenced by western blotting and semi-quantitative reverse transcriptase-polymerase chain reaction. Immunohistochemical analysis and in situ hybridization revealed that plasma cells expressed MMP-8 and -13 focally in periapical granulomas, odontogenic cysts, and malignant plasmacytomas. MMP-8 and MMP-13 from plasma cells can participate in bone organic matrix destruction at sites of chronic inflammation and neoplastic growth. Since MMP-13 was more frequently expressed than MMP-8 in plasma cells of strongly recurring keratocysts and malignant plasmacytomas, it is concluded that plasma cell MMP-13 has a particularly important role in benign and malignant bone-destructive lesions.

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Section: Discussionmentioning

confidence: 77%

Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions

et al. 2001

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“…The recent identification of an enzymatically active, alternatively spliced isoform of MMP‐8 that lacks a signal sequence and is therefore, probably not secreted (Hu et al, 1999) suggests that MMP‐8 gene products may have additional roles to the proteolytic cleavage of extracellular matrix components. The results of a study on the catalytic properties of the standard form of MMP‐8 indicate that this enzyme displays a wide range of interactions with substrates and exhibits a complex interplay among different portions of the enzyme in substrate recognition and processing (Marini et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Expression of matrix metalloproteinase 8 (MMP-8) and tyrosinase-related protein-1 (TYRP-1) correlates with the absence of metastasis in an isogenic human breast cancer model

et al. 2003

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“…probably due to the limited capacity of the furin-like enzyme of the transfected CHO cells to process the excess recombinant protein. Alternative splicing of the mRNA is an uncommon feature among the MMPs, as only a few MMP splice variants have been reported [23][24][25]. It will, therefore, be interesting to investigate the catalytic activity and substrate specificity of the alternatively spliced forms of epilysin towards a biologically relevant substrate.…”

Section: Figure 6 Identification Of Epilysin Mrna By Northern-blot Anmentioning

confidence: 99%

The mouse matrix metalloproteinase, epilysin (MMP-28), is alternatively spliced and processed by a furin-like proprotein convertase

Illman

Keski‐Oja

Parks

et al. 2003

Biochemical Journal

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Epilysin (MMP-28) is a recently identified member of the matrix metalloproteinase (MMP) family. To explore the expression of epilysin in vivo and to gain insight into its biological functions, we have cloned the mouse epilysin cDNA and determined its expression. The amino acid sequence of the mouse protein is 85% identical with the human sequence and contains conserved features such as an RKKR furin-activation sequence following the prodomain. Unexpectedly, we found two alternatively spliced forms of the epilysin mRNA lacking 30 and 72 nt at the beginning of the seventh exon coding for part of the haemopexin domain. Expression of recombinant epilysin in HT-1080 fibrosarcoma cells indicated that epilysin was secreted as a major 48 kDa form and a minor 58 kDa form. Expression of the 58 kDa form was increased by a synthetic furin inhibitor at the expense of the 48 kDa form, suggesting that furin cleaves and activates epilysin. Epilysin mRNA was detected in a number of mouse tissues, with the highest expression in the lung, placenta, heart and uterus, and lower levels in the testis and gastrointestinal tract. The wide expression of epilysin in intact, healthy tissues suggests that this MMP functions in physiological tissue homoeostasis and turnover.

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Identification of a splice variant of neutrophil collagenase (MMP‐8)

Cited by 14 publications

References 16 publications

Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions

Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions

Expression of matrix metalloproteinase 8 (MMP-8) and tyrosinase-related protein-1 (TYRP-1) correlates with the absence of metastasis in an isogenic human breast cancer model

The mouse matrix metalloproteinase, epilysin (MMP-28), is alternatively spliced and processed by a furin-like proprotein convertase

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