ライフサイエンスコーパス: gelatinase A

1 or both MMP-9 and metalloproteinase-2 (MMP-2/gelatinase A).

2 MMP-1 (interstitial collagenase) and MMP-2 (gelatinase A).

3 not with matrix metalloproteinase 2 (MMP-2, gelatinase A).

4 in both the production and release of MMP-2 (gelatinase A).

5 he expression of metalloproteinase-2 (MMP-2, gelatinase A).

6 n lattice (dermal equivalent) secrete active gelatinase A.

7 ses, and by BB3003, a selective inhibitor of gelatinase A.

8 embrane-anchored enzyme and an activator for gelatinase A.

9 th the proenzyme form and the active form of gelatinase A.

10 complete inhibition of activation of latent gelatinase A.

11 rotease that was historically referred to as gelatinase A.

12 iated adipocytes expressed an activated MMP, gelatinase A.

13 ent work shows that these cells also secrete gelatinase A.

14 r mixtures of MMPs such as collagenase 3 and gelatinase A.

15 P-2 binding and subsequent activation of pro-gelatinase A.

16 surface and initiating the activation of pro-gelatinase A.

17 e matrix metalloproteinases (MMP), including gelatinase A (72-kDa type IV collagenase) as inactive zy

18 interstitial collagenase, stromelysin-1, and gelatinase A (72-kDa type IV collagenase).

19 The activity of gelatinase A, a member of the matrix metalloproteinase f

20 the same 63-kDa protein without loss of pro-gelatinase A activation function.

21 h (a furin inhibitor) did not affect the pro-gelatinase A activation mechanism in COS-1 cells cotrans

22 MMP expression might contribute, in part, to gelatinase A activation, which in turn facilitates invas

23 ion of MT-MMP1 is not a prerequisite for pro-gelatinase A activation.

24 Gelatinase A activity is required for maximal proliferat

25 Gelatinase A activity within the fibrous scleras of form

26 In addition, purified active gelatinase A alone is sufficient to induce epithelial-me

27 ARCaP cells also secrete high levels of gelatinase A and B and some stromelysin, which suggests

28 ted in increased secretion and activation of gelatinase A and B.

29 ver, the total expression levels of seprase, gelatinase A and beta1 integrins were not altered.

30 Increased gelatinase A and gelatinase B expression (demonstrated b

31 In particular, MMP-2 and MMP-9 (gelatinase A and gelatinase B, respectively) have been i

32 es and in a tonsillar cell suspension, while gelatinase A and interstitial collagenase activities wer

33 the distribution and relative expression of gelatinase A and its associated inhibitor, tissue inhibi

34 n treatment resulted in the up-regulation of gelatinase A and macrophage metalloelastase gene express

35 we investigated the expression of activated gelatinase A and membrane-type metalloproteinase (MT-MMP

36 NSE) on two matrix metalloproteinases, MMP-2/gelatinase A and MMP-9/gelatinase B, which are known to

37 We also examined gelatinase A and MT-MMP expression in human brain tumor

38 Expression of the matrix metalloproteinases gelatinase A and stromelysin-1 and the serine proteinase

39 Changes in the steady state levels of gelatinase A and TIMP-2 mRNA lead to changes in gelatina

40 The distribution of gelatinase A and TIMP-2 mRNAs was evaluated by in situ h

41 alysis analyses using cDNA probes to chicken gelatinase A and TIMP-2.

42 nsfected into COS-1 cells with cDNAs for pro-gelatinase A and/or furin.

43 ein through the action, at least in part, of gelatinase A and/or stromelysin.

44 y the action of the matrix metalloproteinase gelatinase A and/or stromelysin.

45 used a NIRF substrate for gelatinases (MMP-2/gelatinase-A and MMP-9/gelatinase-B) in apolipoprotein E

46 irst evidence that normal mast cells express gelatinases A and B and suggest pathways by which their

47 Furthermore, gelatinases A and B both colocalize to alpha-chymase-exp

48 levels within 18 h, while the expression of gelatinases A and B remained unchanged, suggesting that

49 expression in rat corneas parallels that of gelatinases A and B, respectively.

50 ctive over stromelysin 1, collagenase 1, and gelatinases A and B, respectively.

51 increases expression and activity of MMP-2 (gelatinase A) and -9 (gelatinase B) in cardiac fibroblas

52 levels of matrix metalloproteinase (MMP)-2 (gelatinase A) and -9 (gelatinase B) were synthesized and

53 forms of matrix metalloproteinase-2 (MMP-2, gelatinase A) and do not react with unrelated proteins i

54 other MMPs (stromelysin-1, stromelysin-3 and gelatinase A) and MMP inhibitors (TIMP-1 and TIMP-2) wer

55 proteinases (MMPs) and, specifically, MMP-2 (gelatinase A) and MMP-9 (gelatinase B) are strongly asso

56 MMP-2 (gelatinase A) and MMP-9 (gelatinase B) were the only two

57 tion analysis was conducted for stromelysin, gelatinase A, and gelatinase B with the various inhibito

58 ates production of interstitial collagenase, gelatinase A, and stromelysin-1 by fibroblasts, and we h

59 d in collagen lattices contain active 62-kDa gelatinase A at least 4-6 h before active enzyme is dete

60 r this inconsistency is that the bulk of the gelatinase A binding depends on its ability to diffuse l

61 An investigation of gelatinase A binding to gelatin produced results that ar

62 en used to analyze the rate of inhibition of gelatinase A by TIMP-2 over a wide range of TIMP-2 conce

63 of inhibition of matrix metalloproteinase-2 (gelatinase A) by tissue inhibitor of metalloproteinase-2

64 med to be matrix metalloproteinase-2 (MMP-2; gelatinase A) by Western blotting and immunoprecipitatio

65 S-1 cells cotransfected with MT-MMP1 and pro-gelatinase A cDNAs.

66 We identified MMP2 as the highly active gelatinase, a class of MMP, in the gonadal WAT of high-f

67 M region that spans the gene encoding MMP-2 (gelatinase A, collagenase type IV;.

68 correlates with expression and activation of gelatinase A during malignant progression in vivo.

69 In situ hybridization confirmed gelatinase A expression by the epithelial cells and the

70 ha-chymase expression are regulated, whereas gelatinase A expression is constitutive.

71 We demonstrate that high level gelatinase A expression is mediated by a unique interact

72 Gelatinase A expression was maximal at 7 days of culture

73 from lattice cultures are unable to convert gelatinase A from the zymogen to its active form.

74 n vivo distribution of type VII collagen and gelatinase A (Gel A) in the developing human epidermis a

75 Unlike gelatinase A, gelatinase B is expressed exclusively by m

76 We have studied the expression of gelatinase A, gelatinase B, interstitial collagenase, ti

77 Gelatinase A, gelatinase B, stromelysin-1, urokinase, TI

78 -1) located in the 5'-flanking region of the gelatinase A gene.

79 Gelatinase A (GL-A) is a matrix metalloproteinase (MMP)

80 xpression of MMP-9 (gelatinase B) and MMP-2 (gelatinase A) have been observed in Alzheimer's disease,

81 eads to the appearance of activated forms of gelatinase A in culture supernatants, and the de novo ex

82 ional implications for the activation of pro-gelatinase A in health and disease.

83 ctivation in vitro and the potential role of gelatinase A in promoting HSC proliferation.

84 bnormal ECM components through activation of gelatinase A in rat corneas.

85 protease, MT1-MMP (MMP-14), and that active gelatinase A is absolutely required for epithelial-mesen

86 Thus, the transcription of gelatinase A is subject to a previously unrecognized int

87 Matrix metalloproteinase-2 (MMP-2; gelatinase A) is known to degrade a broad range of extra

88 transmembrane MMP that activates pro-MMP-2 (gelatinase A), is expressed in human atherosclerotic pla

89 alloproteinase (MMP)-2 (type IV collagenase; gelatinase A), is implicated in tumor metastasis as well

90 te that a discrete matrix metalloproteinase, gelatinase A, is capable of inducing the complex genetic

91 Activated gelatinase A (M(r) 62,000) was induced by ConA in only U

92 A biologic role for the 72-kDa gelatinase A (matrix metalloproteinase 2; MMP-2), beyond

93 We now report that gelatinase A (matrix metalloproteinase-2), produced dire

94 Gelatinase A may also mediate epithelial-mesenchymal tra

95 e in the levels of matrix metalloproteinases gelatinase A (MMP-2) and gelatinase B (MMP-9) after part

96 Gelatinase A (MMP-2) and gelatinase B (MMP-9) are able t

97 and active forms of gelatinase B (MMP-9) and gelatinase A (MMP-2) and to the MMP-9 tissue inhibitor o

98 Gelatinase A (MMP-2) is believed to be necessary for the

99 se in active soluble 17 kDa TNF-alpha and by gelatinase A (MMP-2) upregulation.

100 h in MEE and in adjacent mesenchyme, whereas gelatinase A (MMP-2) was expressed by mesenchymal cells

101 esis of a specific matrix metalloproteinase, gelatinase A (MMP-2), and its activator protease, MT1-MM

102 1, MT1-MMP, (MMP-14) collagenase-3 (MMP-13), gelatinase A (MMP-2), and TIMP-1, -2 and -3] was induced

103 ed immunosorbent assay) were used to measure gelatinase A (MMP-2), gelatinase B (MMP-9) and tissue in

104 (MMP-3), gelatinase B (MMP-9), and activated gelatinase A (MMP-2), in human vascular SMCs by cell con

105 tent inhibitors of stromelysin-1 (MMP-3) and gelatinase A (MMP-2), in the range of 10-50 nM, but poor

106 monoclonal antibodies against the Mr 72,000 gelatinase A (MMP-2), Mr 92,000 gelatinase B (MMP-9), an

107 hritis was found to contain at least 3 MMPs: gelatinase A (MMP-2), stromelysin (MMP-3), and gelatinas

108 ining was performed for collagenase (MMP-1), gelatinase A (MMP-2), stromelysin (MMP-3), TIMP-1, and T

109 ctions were immunostained with antibodies to gelatinase A (MMP-2), stromelysin-1 (MMP-3), and gelatin

110 The wild type protein inhibited gelatinase A (MMP-2), whereas a variant with an alanine

111 ly potent against collagenase-3 (MMP-13) and gelatinase A (MMP-2), while they spared collagenase-1 (M

112 that it is distinct from the chicken 72-kDa gelatinase A (MMP-2).

113 MP-1) and stromelysin (MMP-3), and activated gelatinase A (MMP-2).

114 n (alpha1(I) chain), decorin (core protein), gelatinase-A (MMP-2), stromelysin-1 (MMP-3), and a tissu

115 e that stromelysin-1 (MMP-3), as well as the gelatinases A (MMP-2) and B (MMP-9), processes recombina

116 n core protein), degradative enzymes (MMP-2 [gelatinase-A], MMP-3 [stromelysin-1]), and a tissue inhi

117 ull fibroblasts produce a 2-fold increase in gelatinase A (MMP2) compared with wild-type cells.

118 Intracellular levels of gelatinase A mRNA and protein increase during the cultur

119 Gelatinase A mRNA transcripts were strongly expressed in

120 any family members, including stromelysin-3, gelatinase A, MT-MMP, interstitial collagenase, and stro

121 Gelatinase A, MT1-MMP, and TIMP-2 messenger RNA (mRNA) w

122 These studies examine gelatinase A, MT1-MMP, and TIMP-2 synthesis by HSCs duri

123 Active forms of gelatinase A of 62 kd and 66 kd were secreted by activat

124 (MT-MMP) activate the zymogen form of MMP-2/Gelatinase A on cell surfaces and are expressed in invas

125 thought to be responsible for activation of gelatinase A on the plasma membrane of tumor cells, show

126 ollagenases (MMP-1 and MMP-13), gelatinases (gelatinase A or B), stromelysins (MMP-3 and MMP-11), or

127 kDa type IV collagenase, also referred to as gelatinase A or MMP-2, has been proposed to potentiate t

128 f other metzincins, including collagenase or gelatinases A or B.

129 elysin and gelatinase B but not collagenase, gelatinase A, or tissue inhibitor of metalloproteinases

130 The matrix metalloproteinase gelatinase A plays a central role in several critical ph

131 of prostate-specific antigen (PSA) protein, gelatinase A protein, and POV1 (PB39) cDNA.

132 mRNA and protein for gelatinase A, stromelysin-1 and uPA were weakly induced,

133 Overexpression of YB-1 and AP2 proteins by gelatinase A synthesizing hepatoma HepG2 cells induced a

134 e dissociation of 125I-labeled TIMP-2 from a gelatinase A-TIMP-2 complex using ligand exchange experi

135 s invasion independently of plasminogen, the gelatinase A/TIMP-2 axis, gelatinase B, collagenase-3, c

136 itu hybridization indicated that most of the gelatinase A transcripts were present in the fibrous lay

137 azole urea inhibitors with stromelysin-1 and gelatinase-A, two homologous MMPs that have been implica

138 Gelatinase A was immunolocalized to the epithelium and s

139 is indicated that the relative expression of gelatinase A was increased by 128% in deprived eyes (P =

140 Gelatinase A was less effective in processing pIL-1 beta

141 gelatinase A, whereas the activated form of gelatinase A was only seen in metastatic lung adenocarci

142 MT1-MMP and gelatinase A were co-localized to sites of active epithe

143 TIMP-3 mRNA while stromelysin-3, TIMP-2 and gelatinase A were seen in the overlying connective tissu

144 of collagenase I and stromelysin I, but not gelatinase A, were inhibited in the mutant STAT3 transfe

145 samples examined contained a latent form of gelatinase A, whereas the activated form of gelatinase A

146 ntral cornea contained the proenzyme form of gelatinase A, whereas the peripheral cornea contained bo

147 will bind selectively to stromelysin-1 over gelatinase-A which is gratifying given the high degree o

148 llate cells (HSCs) are a potential source of gelatinase A, which accumulates in fibrotic livers.

149 MT1-MMP and enhanced secretion of activated gelatinase A, which reached a maximum of 44.4% of the to