ライフサイエンスコーパス: hemopexin

1 s after exposure to hypoxia and heme or heme/hemopexin.

2 plasma retinol binding protein, albumin, and hemopexin.

3 nt importance in cellular protection by heme-hemopexin.

4 es of cellular events upon encountering heme-hemopexin.

5 n, is involved in use of hemoglobin and heme-hemopexin.

6 HO-1 remains responsive to induction by heme-hemopexin.

7 ermediate between those of serum albumin and hemopexin.

8 iron, the chaperone proteins haptoglobin and hemopexin.

9 ated by treatment with either haptoglobin or hemopexin.

10 LDI-MS analysis for a low abundance protein, hemopexin.

11 ue, haptoglobin, or the heme-binding protein hemopexin.

12 osine residues and one tryptophan residue of hemopexin.

13 ickle mice by treating them with recombinant hemopexin.

14 ich was similarly nitrated in rabbit and rat hemopexins.

15 me with lipopolysaccharide was suppressed by hemopexin, a plasma heme-binding protein.

16 Hemopexin also inhibited bacterial hemin binding.

17 umin), our observations further suggest that hemopexin, an abundant protein with a serum concentratio

18 Hemopexin and a putative hemopexin receptor on hepatocyt

19 ects were largely blocked by heme-scavenging hemopexin and by the PS antagonist annexin-a5, in vitro

20 a genetic dissection of the functions of the hemopexin and catalytic domains of a canonical MMP in Dr

21 the heme and hemoglobin scavenger proteins, hemopexin and haptoglobin.

22 Degradation of hemopexin and transferrin in human serum by Kgp was also

23 ns (gingipains R) were also found to degrade hemopexin and transferrin in serum; however, this was ob

24 proteins (serum amyloid A, haptoglobin, and hemopexin) and depleted of paraoxonase-1 after SFA-HFD i

25 ons of the endogenous chelators haptoglobin, hemopexin, and alpha1- microglobulin.

26 APP genes, including thiostatin, fibrinogen, hemopexin, and haptoglobin.

27 organism to degrade hemoglobin, haptoglobin, hemopexin, and transferrin but also with an increase in

28 neutrophil gelatinase-associated lipocalin, hemopexin, and transferrin were increased in FtH(PT-/-)

29 tyrosines reside in the heme-binding site of hemopexin, and we found that one, Tyr-199, interacts dir

30 ibitor p21(WAF1/CIP1/SDI1) generated by heme-hemopexin appear to be of paramount importance in cellul

31 Utilization of heme-hemopexin as a source of heme by Haemophilus influenzae

32 n bound to haptoglobin and heme complexed to hemopexin as heme sources; however, the mechanism by whi

33 rum albumin (HSA) and myoglobin (Mb) but not hemopexin as iron sources.

34 e development of human plasma-derived Hp and hemopexin as therapeutics for patients with excessive in

35 moproteins hemoglobin and myoglobin, but not hemopexin, as iron sources for bacterial growth.

36 hemoglobin, hemoglobin-haptoglobin, or heme-hemopexin, as iron sources.

37 mice, the administration of human exogenous hemopexin attenuates the inflammatory phenotype of macro

38 -binding proteins TbpA and TbpB, the 100-kDa hemopexin-binding protein HxuA, and the hemoglobin-bindi

39 h stimulation seen with 0.1-0.75 microM heme-hemopexin but HO-1 remains responsive to induction by he

40 Treatment with haptoglobin or hemopexin but not albumin improved the survival rate and

41 reatment with exogenous human haptoglobin or hemopexin can ameliorate adverse effects of resuscitatio

42 bound to haptoglobin and hemin complexed to hemopexin can be used as heme sources, indicating that P

43 ia were able to grow on Hb, heme, myoglobin, hemopexin, catalase, human and bovine serum albumin-heme

44 uA mutant was unable to utilize soluble heme-hemopexin complexes for growth in vitro unless soluble H

45 This protection is sustained by heme-hemopexin complexes in biological fluids that resist oxi

46 uenzae type b culture supernatant bound heme-hemopexin complexes in solution.

47 ults indicated that the heme present in heme-hemopexin complexes is rendered accessible to H. influen

48 Significantly, heme binding by hemopexin declined as tyrosine nitration proceeded in vi

49 The biochemical responses to heme-hemopexin depend on its extracellular concentration and

50 is critical for proMMP-2 activation, whereas hemopexin-dependent dimerization is important for degrad

51 Final studies show that hemopexin directly interacts with FLVCR, which also help

52 The structure of MT1-MMP includes the hemopexin domain (PEX) that is distinct from and additio

53 includes a catalytic domain, a hinge, and a hemopexin domain (PEX), which are followed by a transmem

54 a non-proteolytic mechanism and the proMMP-9 hemopexin domain (PEX9).

55 domains, we confirmed the importance of the hemopexin domain also in primary organoids of the mammar

56 ctivity of MMP3 as the central player to its hemopexin domain and add a new dimension to HSP90beta's

57 Thus, we find that this MMP hemopexin domain has an apparent specialization for tiss

58 Moreover, the hemopexin domain is also required for MT1-MMP-mediated i

59 ty to TIMP2-inhibited MMP-2, while the MMP-2 hemopexin domain is not required for reactivation.

60 Here we show that the conserved hemopexin domain is required for MT1-MMP-mediated invasi

61 atrix remodeling of the tracheal system, the hemopexin domain is required specifically for tissue inv

62 null alleles with alleles that have specific hemopexin domain lesions, and we also examine phenotypes

63 nding domain of alpha-2-macroglobulin or the hemopexin domain of matrix metalloproteinase 9) induces

64 P-3 with the hinge region and the C-terminal hemopexin domain of MMP-1 did not express any collagenol

65 is substrate by decreasing K(m), just as the hemopexin domain of MMP-1 enhances its triple helical pe

66 The pattern of binding of the free hemopexin domain of MMP-13 was similar to that of the fu

67 that there are two TIMP binding sites on the hemopexin domain of MMP-2: one with high affinity that i

68 racellular matrix component gelatin, and the hemopexin domain of MMP-9 (PEX9) inhibits this degradati

69 protein (MMP-9-PEX), which includes only the hemopexin domain of MMP-9, replicated the activities of

70 An antibody targeting the hemopexin domain of MMP-9, which mediates the interactio

71 xtracellularly, and its interaction with the hemopexin domain of MMP3 is critical for invasion.

72 The noncatalytic hemopexin domain of MMP9 binds to the low-density lipopr

73 , it is proposed that cross-talk between the hemopexin domain of MT1-MMP and adjacent cell surface mo

74 ny component of this pathway, including MMP9 hemopexin domain or claudin-1 siRNA, enables an opioid p

75 Thus, targeting the MMP-14 hemopexin domain represents a novel approach to inhibit

76 vasion and branching, we show that it is the hemopexin domain that directs these processes.

77 N-terminal catalytic domain; 2) a C-terminal hemopexin domain that regulates substrate recognition as

78 an antibody preventing binding of the MMP-9 hemopexin domain to beta1-integrin.

79 The presence of an intact active site and hemopexin domain were required for full angiogenesis-ind

80 her MMP genes, with its C-terminal half (the hemopexin domain) encoded by 4 instead of 6 exons, as in

81 rodomain, (2) the hinge region preceding the hemopexin domain, and (3) the hemopexin domain.

82 s, mainly in the relative orientation of the hemopexin domain, between the pro form and active form o

83 that RWTNNFREY, together with the C-terminal hemopexin domain, is essential for collagenolytic activi

84 egrin alpha(v)beta3 binding to MMP2, via its hemopexin domain, result in significantly reduced cellul

85 PAR1 cleavage by MMP-2 by binding the MMP-2 hemopexin domain, thus favoring the interaction of the e

86 An exosite in the hemopexin domain, which binds the leucine 10 residues C-

87 preceding the hemopexin domain, and (3) the hemopexin domain.

88 ctivity of MMP14 but absolutely required the hemopexin domain.

89 MMP in addition to the previously identified hemopexin domain.

90 bition of either the catalytic domain or the hemopexin domain.

91 Deletion of the hemopexin domains in MT1-, MT2-, MT3-, MT5-, and MT6-MMP

92 The hemopexin domains of MMP-12 and -9 each increased k(cat)

93 asiveness in vivo, our data suggest that the hemopexin domains of MT-MMPs should be targeted for the

94 ha(2) I domain interacts with the linker and hemopexin domains of pro-MMP-1, not with the pro-domain.

95 the cooperative action of its catalytic and hemopexin domains.

96 ecific participation of MT-MMP catalytic and hemopexin domains.

97 n K, Kgp) can efficiently cleave hemoglobin, hemopexin, haptoglobin, and transferrin.

98 Together, these data argue that hemopexin has a role in assuring systemic iron balance d

99 l Hb and the hemin-scavenger proteins Hp and hemopexin have a strong potential to neutralize the adve

100 to utilize hemoglobin and complexes of heme-hemopexin, heme-albumin, and hemoglobin-haptoglobin and

101 f apolipoprotein A-I (Apo A-I), haptoglobin, hemopexin, hemoglobin, and myeloperoxidase (MPO) were me

102 After 24 h exposure to 10 microM heme-hemopexin, Hepa cells become refractory to the growth st

103 fucosylation and apply it to a comparison of hemopexin (HPX) and complement factor H (CFH), two liver

104 henotypic feature of GS) and iron, decreased hemopexin (Hpx) and Hpt and in up-regulated biliverdin r

105 that homodimerization of MT1-MMP through its hemopexin (Hpx) domain is essential for cleaving type I

106 risingly, in a nonproteolytic manner via its hemopexin (HPX) domain.

107 Hemopexin (hpx) facilitates the degradation of extracell

108 its scavenger proteins, haptoglobin (Hp) and hemopexin (Hx) are significantly increased in apoA-1-con

109 Hemopexin (Hx) is a plasma heme scavenger able to preven

110 Hemopexin (Hx) is an acute-phase protein synthesized by

111 The synergy was strongly suppressed by hemopexin (Hx), an endogenous heme-binding plasma protei

112 roteomic analysis, alpha1-antitrypsin (AAT), hemopexin (HX), and gelsolin (GSN), and tested against c

113 t low (0.01-1 microM) concentrations of heme-hemopexin increase, albeit transiently, the protein carb

114 y state that was inhibited by haptoglobin or hemopexin infusion.

115 a suggest that therapeutic administration of hemopexin is beneficial to counteract heme-driven macrop

116 We propose that during inflammation, apo-hemopexin is nitrated and oxidated in niches of the body

117 However, apo-hemopexin is vulnerable to inactivation by reactive nitr

118 old more efficient when the medium contained hemopexin (K(d) < 1 pm) compared with albumin (K(d) = 5

119 On the other hand, hemopexin-less MT1-MMP fails to promote cell invasion in

120 In fact, hemopexin-less MT5- and MT6-MMP activate proMMP2 better

121 triple-helix is bound initially by the MMP-1 hemopexin-like (HPX) domain via a four amino acid stretc

122 flexibility between the catalytic (CAT) and hemopexin-like (HPX) domains.

123 tivation were not affected by removal of the hemopexin-like C-terminal domain.

124 ant DNA approaches, we demonstrated that the hemopexin-like domain and a nonenzymatic component of th

125 the cloned MMP does not contain a consensus hemopexin-like domain because it lacks a critical trypto

126 epitope in the protein's carboxyl-terminal, hemopexin-like domain identified a post-translational cl

127 roles of specific residues within the MMP-1 hemopexin-like domain in substrate binding and turnover.

128 included the catalytic domain but lacked the hemopexin-like domain lost the proteolytic capacity; how

129 termined that both the linker domain and the hemopexin-like domain of MMP-1 were required for optimal

130 doxycycline disrupts the conformation of the hemopexin-like domain of MMP-13 and the catalytic domain

131 The C-terminal hemopexin-like domain of MMP-2, which interferes with th

132 The hemopexin-like domain of MMP2, which interferes with MMP

133 tin is greatly facilitated by the C-terminal hemopexin-like domain of the enzyme whereas the specific

134 cysteine residue, was not cleaved within the hemopexin-like domain when expressed in COS-7 cells.

135 nt of the short form (lacking the C-terminal hemopexin-like domain) of HS (sHS) has been prepared and

136 (iv) a zinc-binding catalytic domain, (v) a hemopexin-like domain, (vi) a 24-residue hydrophobic dom

137 ncated forms of MMP-8 and MMP-13 lacking the hemopexin-like domain, and a mutant form of truncated MM

138 ent of MMP-2, which comprises the C-terminal hemopexin-like domain, termed PEX, prevents this enzyme

139 istinct residues in blades III and IV of its hemopexin-like domain, while binding of collagen-like tr

140 te, a catalytic domain, a hinge-region and a hemopexin-like domain.

141 c domain with an HEIGHTLGLTH sequence, and a hemopexin-like domain.

142 eats, a catalytic zinc binding region, and a hemopexin-like domain.

143 at room temperature is achieved without the hemopexin-like domain.

144 in protein containing both a catalytic and a hemopexin-like domain.

145 ed MMP genes, whereas the exons encoding the hemopexin-like domains are similar to those of most othe

146 udies indicates that the MMP-1 catalytic and hemopexin-like domains collaborate in collagen catabolis

147 nces, and subsequently the catalytic and the hemopexin-like domains, have been performed.

148 anking the catalytic center and the carboxyl hemopexin-like region.

149 curring human plasma proteins haptoglobin or hemopexin may have beneficial effects in conditions of s

150 ion coexists with blood degradation and that hemopexin may play a role in controlling inflammation in

151 ain K to cleave hemoglobin, haptoglobin, and hemopexin may provide P. gingivalis with a usable source

152 red blood cells, treatment with haptoglobin, hemopexin, or albumin did not cause harmful effects.

153 RBCs were given a coinfusion of haptoglobin, hemopexin, or albumin.

154 The hemopexin (PEX) domain of MMP-14 has been proposed as th

155 We previously demonstrated that the hemopexin (PEX) domain of MMP-9 is a prerequisite for en

156 In this work, compounds that target the hemopexin (PEX) domain of MMP-9 were identified using an

157 iations with erythrocyte count, haptoglobin, hemopexin, plasma heme, expression of receptors for heme

158 Hemopexin protects against heme toxicity in hemolytic di

159 Hemopexin protects cells lacking hemopexin receptors by

160 further demonstrate that the heme scavenger hemopexin protects reticulo-endothelial macrophages from

161 Hemopexin and a putative hemopexin receptor on hepatocyte membranes may mediate t

162 Hemopexin protects cells lacking hemopexin receptors by tightly binding heme abrogating i

163 However, whether there are sufficient hemopexin receptors on rat hepatocytes to account for th

164 nonspecific heme uptake, whereas cells with hemopexin receptors undergo a series of cellular events

165 Pharmacologic inhibition of TLR4 and hemopexin replacement therapy prior to hemin infusion pr

166 and endothelial cells, potentially impairing hemopexin's protective extracellular antioxidant functio

167 c sites and the fibronectin type II-like and hemopexin/TIMP2 binding domains.

168 Hemopexin, transferrin, mammaglobin B, and secretoglobin

169 e cell surface in the absence of the MT1-MMP hemopexin, transmembrane, and cytosolic tail domains.

170 y is not confined strictly to the catalytic, hemopexin, transmembrane, or cytosolic domain sequences

171 Hemopexin treatment is a promising novel therapy to prot

172 porphyrin export improved with extracellular hemopexin (versus albumin), our observations further sug

173 the catalytic domain and carboxyl-terminal "hemopexin/vitronectin-like" domain.

174 rosine nitration of in vivo samples and when hemopexin was incubated in vitro with nitrating nitrite/

175 s, levels of serum albumin, transferrin, and hemopexin were found up to 100 times higher than control

176 esize the scavenger proteins haptoglobin and hemopexin, which bind extracellular hemoglobin and heme,

177 eme transport since cobalt-protoporphyrin IX-hemopexin, which binds to the receptor and activates sig

178 YCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and ra

179 Plasma levels of hemopexin, which were decreased in women with preeclamps

180 NK) is rapidly activated by 2-10 microM heme-hemopexin, yet the increased intracellular heme levels a