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首页> 美国卫生研究院文献>Biochemical Journal >Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A gelatinase B and collagenase 3.
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Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A gelatinase B and collagenase 3.

机译：基于膜型1基质金属蛋白酶的基质金属蛋白酶激活级联反应的诱导：明胶酶A明胶酶B和胶原酶3的相关激活。

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摘要

SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by Western blotting using a specific polyclonal antibody raised against recombinant human procollagenase 3. Oncostatin M enhanced the interleukin-1-induced production of procollagenase 3, whereas interleukin-4 decreased procollagenase 3 synthesis. The enzyme was latent except when the cells had been treated with concanavalin A, when a processed form of 48 kDa, which corresponds to the active form, was found in the culture medium and collagenolytic activity was detected by degradation of 14C-labelled type I collagen. The concanavalin A-induced activation of procollagenase 3 coincided with the processing of progelatinase A (matrix metalloproteinase-2) by the cells, as measured by gelatin zymography. In addition, progelatinase B (matrix metalloproteinase-9) was activated when gelatinase A and collagenase 3 were in their active forms. Concanavalin A treatment of SW1353 cells increased the amount of membrane-type-1 matrix metalloproteinase protein in the cell membranes, suggesting that this membrane-bound enzyme participates in an activation cascade involving collagenase 3 and the gelatinases. This cascade was effectively inhibited by tissue inhibitors of metalloproteinases-2 and -3. Tissue inhibitor of metalloproteinases-1, which is a much weaker inhibitor of membrane-type 1 matrix metalloproteinase than tissue inhibitors of metalloproteinases-2 and -3 [Will, Atkinson, Butler, Smith and Murphy (1996) J. Biol. Chem. 271, 17119-17123], was a weaker inhibitor of the activation cascade.
机译：在存在白介素-1，伴刀豆球蛋白A或PMA的情况下培养的SW1353软骨肉瘤细胞会分泌前胶原酶3（基质金属蛋白酶-13）。使用针对重组人原胶原酶3的特异性多克隆抗体，通过Western印迹在培养基中检测到该酶。制瘤素M增强了白介素1诱导的原胶原酶3的产生，而白介素4降低了原胶原酶3的合成。该酶是潜伏的，除了当用刀豆球蛋白A处理细胞时，在培养基中发现了与活性形式相对应的48 kDa加工形式，并且通过降解14C标记的I型胶原蛋白检测到了胶原蛋白水解活性。 。用明胶酶谱法测定，伴刀豆球蛋白A诱导的前胶原酶3的激活与细胞对明胶酶A（基质金属蛋白酶-2）的处理同时发生。此外，当明胶酶A和胶原酶3处于活性形式时，明胶酶B（基质金属蛋白酶9）被激活。伴刀豆球蛋白A处理SW1353细胞增加了细胞膜中1型膜基质金属蛋白酶蛋白的含量，表明该膜结合酶参与了涉及胶原酶3和明胶酶的激活级联反应。该级联被金属蛋白酶-2和-3的组织抑制剂有效抑制。金属蛋白酶-1的组织抑制剂，其比金属蛋白酶-2和-3的组织抑制剂弱得多的膜型1基质金属蛋白酶的抑制剂[Will，Atkinson，Butler，Smith和Murphy（1996）J.Biol.Chem.Sci。化学271，17119-17123]是激活级联的较弱抑制剂。

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