Primary structure of a 15‐kDa protein from rat intestinal epithelium

KANDA, Tatsuo; Okada, Shoji; TOMOT, Masaaki; Matsubara, Y.; Ono, Teruo

doi:10.1111/j.1432-1033.1991.tb15969.x

Cited by 5 publications

(9 citation statements)

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“…Although I-1SP shows similarity with FABP, endogenous fatty acid analysis and an in vitro binding study with Lipidex have shown that I-15P has little ability to bind to a saturated long-chain fatty acid (palmitate) [4]. The present results with recombinant human 1-1 SP were consistent with our previous findings.…”

Section: Discussionsupporting

confidence: 83%

“…Previously, we hypothesized, based on its localization, that I-15P was involved in the reabsorption of bile acids, and preliminarily examined its binding ability to chenodeoxycholate [4]. However, we could not obtain evidence of its binding to this bile acid under our conditions.…”

Section: Discussioncontrasting

confidence: 43%

“…The probe used was a 258-bp fragment (nucleotides 202-459 of human I-15P cDNA) isolated by PCR amplification as previously described [6]. [4] are indicated. The sequences and their sources are as follows: rat I-1SP 161, L-FABP 1191, H-FABP [20], I-FABP 1211, aP2 1221, CRBP [23], and mP2 [24].…”

Section: Methodsmentioning

confidence: 99%

“…revealed its low affinity for a long-chain fatty acid [4]. Recently, Gong et al [I I] reported that the protein purified from rat ileum, termed the ileal bile-acid-binding protein (I-BABP), was identical with 1-1 SP in primary structure.…”

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confidence: 99%

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Molecular Cloning, Expression, and Characterization of a Human Intestinal 15‐kDa Protein

Fujita

Fujii

Kanda

et al. 1995

European Journal of Biochemistry

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We have isolated a cDNA encoding a human intestinal IS-kDa protein (I-ISP) from a human ileal i g t 11 cDNA library, using a full-length rat I-1SP cDNA. One clone encompassed 571 nucleotides and encoded a 128-amino-acid protein with a calculated molecular mass of 1435.5 Da. The deduced amino acid sequence of human I-1SP showed high similarity to the rat counterpart (78'%), mouse ileal lipidbinding protein (80%) and porcine gastrotropin (75%). It also exhibited 36% similarity to human liver fatty-acid-binding protein (L-FABP). Northern blot analysis of human 1-1 SP revealed a single transcript only in ileum. however, the reverse-transcription/PCR demonstrated expression in ovary and placenta, but it was much lower than in ileum. Transformation of Escherichia coli with the I-1SP cDNA resulted in the efficient expression of a protein that was identical to the ileal cytosolic 1-15P. In vitrz, binding studies revealed that the bacterially expressed recombinant I-1SP showed much lower affinities for palmitate and oleate than L-FABP. However, it showed similar affinity for taurocholate, compared with a control, BSA. Comparison of the structural features of human I-1SP and human L-FABP suggested that loss of a long a-helix region and hydrophobic profile of I-1SP may be attributable to a unique ligandbinding specificity of I-ISP.

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Section: Discussionsupporting

confidence: 83%

Section: Discussioncontrasting

confidence: 43%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular Cloning, Expression, and Characterization of a Human Intestinal 15‐kDa Protein

Fujita

Fujii

Kanda

et al. 1995

European Journal of Biochemistry

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show abstract

“…To date, several FABPs with different chemical structure and tissue distribution designated as liver (hepatic) FABP (CHAN et al, 1985), heart FABP (OFFNER et al, 1988), intestinal FABP (ALPERS et al, 1984), adipocyte P2 protein (MATARESE et al, 1990), myelin P2 protein (SUZUKI et al, 1982), and gastrotropin (WALZ et al, 1988) have been reported. FABPs are present in the cytosole and are thought to play an important role in the transport and metabolism of fatty acids (TIPPING and KETTERER, 1981;COOPER et al, 1987) Recently, KANDA et al (1991) purified a 15 kDa protein (rat I-15P) from the rat intestinal epithelium. Rat I-15P is thought to be a new member of the FABP family, based on its structural feature and amino acid sequence similar to porcine gastrotropin .…”

mentioning

confidence: 99%