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

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

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

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

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

9 complete inhibition of activation of latent gelatinase A.

10 rotease that was historically referred to as gelatinase A.

11 iated adipocytes expressed an activated MMP, gelatinase A.

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

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

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

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

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

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

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

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

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

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

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

23 Gelatinase A activity is required for maximal proliferat

24 Gelatinase A activity within the fibrous scleras of form

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

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

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

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

29 Increased gelatinase A and gelatinase B expression (demonstrated b

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

70 Gelatinase A expression was maximal at 7 days of culture

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

92 Gelatinase A may also mediate epithelial-mesenchymal tra

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

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

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

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

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

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

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

100 1, MT1-MMP, (MMP-14) collagenase-3 (MMP-13), gelatinase A (MMP-2), and TIMP-1, -2 and -3] was induced

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

117 Gelatinase A mRNA transcripts were strongly expressed in

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

136 Gelatinase A was immunolocalized to the epithelium and s

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

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

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

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

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

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

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

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

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

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

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