Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0042384 (vasculitis)
 20,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Wound healing is characterized by hemostasis, re-epithelialization, granulation tissue formation, and remodeling of the extracellular matrix. Matrix metalloproteinases and their specific inhibitors, TIMPs, contribute to these events. We investigated a total of 47 samples of normally healing wounds, chronic venous ulcers, ulcerative vasculitis, and suction blisters using immunohistochemistry and in situ hybridization, to clarify the role of TIMPs in normal and aberrant wound repair. Expression of TIMP-1 and -3 mRNAs was found in proliferating keratinocytes in 3- to 5-day-old normally healing wounds, whereas no epidermal expression was detected in chronic ulcers. However, TIMP-3 protein was found in the proliferating epidermis in 20 of 24 samples representing both full-thickness acute and chronic wounds. TIMP-1 and TIMP-3 also were abundantly expressed by spindle-shaped, fibroblast-like, and plump, macrophage-like stromal cells, as well as by endothelial cells. In normally healing wounds, TIMP-2 protein localized under the migrating epithelial tip and to the stromal tissue under the eschar more frequently than in chronic ulcers. Occasional staining for TIMP-4 protein was detected in stromal cells of chronic ulcers near blood vessels. Our results indicate that TIMP-1 and TIMP-3 may be involved both in the regeneration of the epidermis by stabilizing the basement membrane zone and in the regulation of stromal remodeling and angiogenesis of the wound bed. Lack of TIMP-2 near the migrating epithelial wound edges might contribute to uncontrolled activity of MMP-2 in chronic ulcers. We conclude also that TIMPs are temporally and spatially tightly regulated and that the imbalance between metalloproteinases and TIMPs-1, -2, and -3 may lead to delayed wound healing.
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PMID:Differential expression of tissue inhibitors of metalloproteinases (TIMP-1, -2, -3, and -4) in normal and aberrant wound healing. 1041 98

Kawasaki disease (KD) is an acute febrile vasculitis that predominantly affects infants and young children. Tissue inhibitors of matrix metalloproteinases (TIMPs) comprise a family of four members, of which TIMP4 is characterized by its restriction to cardiovascular structures. In KD pathophysiology, TIMP4 is considered to be involved in the development of coronary artery lesions (CALs). Therefore, this study investigated single-nucleotide polymorphisms (SNPs) of the TIMP4 gene as risk factors for KD with CALs in Korean children. To observe this association, two SNPs (rs3755724, -55C/T, promoter; rs17035945, 3'-untranslated region) were genotyped in TIMP4 using direct sequencing. There were no SNPs in the coding region of TIMP4, and two SNPs were selected in the exon and promoter regions. This study recruited 250 control and 101 KD subjects. For data analysis, SNPStats, SNPAnalyzer, and Helixtree programs were used. These SNPs were not associated with KD. However, in the recessive model, a significant association was found between rs3755724 and the development of CALs in KD (P = 0.02; odds ratio, 0.31; 95% confidence interval, 0.11-0.85). The minor allele (C) of rs3755724 showed the susceptibility of CALs to risk in KD patients. These results suggest that TIMP4 is related to the development of KD with CALs in Korean children.
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PMID:Promoter polymorphism (rs3755724, -55C/T) of tissue inhibitor of metalloproteinase 4 (TIMP4) as a risk factor for Kawasaki disease with coronary artery lesions in a Korean population. 1904 77