Association of TIMP-2 with extracellular matrix exposed to mechanical stress and its co-distribution with periostin during mouse mandible development
Association of TIMP-2 with extracellular matrix exposed to mechanical stress and its co-distribution with periostin during mouse mandible development
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DOI：
10.1007/s00441-007-0439-x
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发表时间：
2007-06
影响因子：
3.6
通讯作者：
N. Yoshiba;K. Yoshiba;A. Hosoya;M. Saito;Takamasa Yokoi;T. Okiji;N. Amizuka;H. Ozawa
中科院分区：
文献类型：
--
作者：
N. Yoshiba;K. Yoshiba;A. Hosoya;M. Saito;Takamasa Yokoi;T. Okiji;N. Amizuka;H. Ozawa
基质重塑是由基质金属蛋白酶（MMPs）和组织金属蛋白酶抑制剂（TIMPs）调控的。Periostin最初在小鼠成骨细胞文库中发现，在细胞粘附和迁移以及机械应力诱导的基质重塑中发挥作用。在本研究中，我们分析和比较了TIMP-2和骨膜蛋白在小鼠下颌骨发育过程中的分布规律。对胚胎13-16天、出生后第2天（P2）、第35天和12周龄小鼠的连续冷冻切片进行TIMP-2和骨膜蛋白的免疫组织化学染色。TIMP-2和骨膜蛋白在下颌骨发育过程中表现出惊人的相似。从磨牙芽期到早期钟期，TIMP-2和骨膜蛋白在舌侧和基底膜前侧以及邻近颌间质上高度表达。在产前和产后切牙，对牙尖环和牙滤泡基底膜进行TIMP-2和骨膜蛋白免疫染色。在出生后阶段，TIMP-2和骨膜蛋白明显局限于牙龈组织、牙周韧带和肌腱的细胞外基质（ECM）（所有机械应变接受者）。而骨膜素仅在毛囊内根鞘下部检测到。在抗timp -2抗体条件培养基中培养的P2牙龈，其牙周素染色明显减少。我们认为TIMP-2和periostin共同分布在机械力作用下的ECM上，并协同起ECM调节剂的作用。
Matrix remodeling is regulated by matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Periostin, originally identified in a mouse osteoblastic library, plays a role in cell adhesion and migration and in mechanical stress-induced matrix remodeling. In this study, we analyzed and compared the distribution patterns of TIMP-2 and periostin during mouse mandible development. Immunohistochemical staining for TIMP-2 and periostin was carried out on serial cryosections obtained from mice at embryonic days 13–16, postnatal day 2 (P2), P35, and 12 weeks of age. TIMP-2 and periostin exhibited a strikingly similar protein distribution during mandible development. From bud to early bell stages of molars, TIMP-2 and periostin were highly expressed on the lingual and anterior sides of the basement membrane and on the adjacent jaw mesenchyme. In pre- and postnatal incisors, the basement membrane of the apical loop and dental follicle was immunostained for TIMP-2 and periostin. At postnatal stages, TIMP-2 and periostin were prominently confined to the extracellular matrix (ECM) of gingival tissues, periodontal ligaments, and tendons (all recipients of mechanical strain). However, periostin was solely detected in the lower portion of the inner root sheath of hair follicles. Gingiva of P2 cultured in anti-TIMP-2 antibody-conditioned medium showed markedly reduced staining of periostin. We suggest that TIMP-2 and periostin are co-distributed on ECM exposed to mechanical forces and coordinately function as ECM modulators.