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- Qian, Bi-Feng, et al.
(author)
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Both substance P and its receptor are expressed in mouse intestinal T lymphocytes
- 2001
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In: Neuroendocrinology. - : S. Karger AG. - 0028-3835 .- 1423-0194. ; 73:5, s. 358-368
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Journal article (peer-reviewed)abstract
- Substance P (SP), one of the most prevalent neuropeptides in gut, has been reported to have potent immune modulatory effects as a proinflammatory agent. The synthesis of SP and SP receptor expression in intraepithelial and lamina propria T lymphocytes of mouse intestine was investigated. Using RT-PCR analysis, it was demonstrated that SP receptor mRNA was exclusively expressed in intraepithelial and lamina propria T lymphocytes as well as their purified CD4+, CD8+ and CD4-CD8-CD3+ subsets. Messenger RNAs (mRNAs) for the two precursors of SP, beta and gamma-preprotachykinin-A, were also detected. These results were consistent in lymphocytes from both epithelium and lamina propria of small and large intestines, although the frequencies and/or intensities of mRNA expression varied. However, none of the findings could be repeated in splenic T lymphocytes. Activation of splenocytes with anti-CD3epsilon-chain mAb and PMA did not induce expression of SP or its receptor mRNAs. Furthermore, both cytoplasmic and surface-bound SP was demonstrated in intestinal T lymphocytes using dual color immunocytochemistry and immunoflow cytometry. In vitro treatment with SP did not significantly change the size of the SP-immunoreactive T cell population, indicating the presence of SP receptor on intestinal T lymphocytes as well as in vivo binding of endogenously released SP. Our data suggest that SP production and SP receptor expression are distinctive for mouse intestinal mucosal immunity and that SP may act as a modulator of an ongoing controlled inflammation in normal gut, by acting through its specific receptor on T lymphocytes in an autocrine and/or paracrine pattern.
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- Zhang, L., et al.
(author)
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Transition from triple helix to coil of Lentinan in solution measured by SEC, viscometry, and C-13 NMR
- 2002
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In: Polymer journal. - : Springer Science and Business Media LLC. - 0032-3896 .- 1349-0540. ; 34:6, s. 443-449
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Journal article (peer-reviewed)abstract
- Lentinan, beta-(1 --> 3)-D-glucan with (1 --> 6) branching, was isolated from Lentinus edodes. Weight-average molecular weight M-w radius of gyration < s(2) > (1/2) and intrinsic viscosity [eta] of Lentinan in 0.2 M NaCl aqueous solution, dimethylsulfoxide (DMSO) and water/DMSO mixtures were measured by light scattering (LS), size exclusion chromatography (SEC) combined with LS, and viscometry. The results indicated that the glucan exists mainly as triple-helical chains in 0.2 M NaCl aqueous solution and water/DMSO mixtures with over 20 wt% water content, and as single-flexible chain in DMSO. The data from SEC-LS, viscosity and C-13 NMR measurements proved strongly that the helix-coil conformation transition occurred in a narrow range from 80 to 85 wt% DMSO aqueous solution, accompanying with obvious changes of M-w, < s(2) >(1/2)(z), [eta] as well as signals of C6 and C6(s). The transition of Lentinan in water/DMSO mixture was irreversible. The difference in C-13 NMR spectra for the triple-helical and coil conformations was the disappearance of the signals of C3 in beta-(1 --> 3)- linked backbone and the enhancement in relative intensities of glucose substituted C6s in the helix state, as well as the appearance of an asymmetric and broad peak of C6 in the intermediate of the conformation change. This suggests that the immobilization of the backbone by binding with intra and intermolecular hydrogen bonds resulted in the loss of the signals of its carbon atoms in the triple helix state. An overcoating cylinder model composed of the beta-(1 --> 3)- linked backbone as helix core and the side chains as rotatable overcoat was proposed to illustrate the triple-helical conformation and its transition in the solution.
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- Zhou, G Q, et al.
(author)
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Pregnancy-specific glycoprotein (PSG) in baboon (Papio hamadryas) : family size, domain structure, and prediction of a functional region in primate PSGs.
- 2001
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In: Biology of Reproduction. - 0006-3363 .- 1529-7268. ; 64:1, s. 90-9
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Journal article (peer-reviewed)abstract
- Pregnancy-specific glycoprotein (PSG) constitutes a major component of serum of pregnant women and appears to be essential for a successful pregnancy. Its function is, however, still unknown. Because of the evolutionary divergence between human and rodent PSG, functional studies may require a primate animal model. We have characterized PSG transcripts in a baboon placenta cDNA library and analyzed baboon genomic DNA. The main PSG isoform had the domain structure N-A1-B2-C similar to the human type IIa isoform. The type I isoform (N-A1-A2-B2-C) was also expressed. Fifteen similar PSG genes were identified of which at least nine were simultaneously expressed in third trimester baboon placenta. Thus, the baboon PSG family was as complex as that of humans. Recombinant baboon PSG (isoform IIa) had a molecular weight of 38 kDa and reacted with antibodies against human PSG. Comparative analysis of 43 N-domain amino acid sequences of PSG from four species and nine primate carcinoembryonic antigen subgroup N domain sequences identified a number of residues in the GFCC'C" ss-sheet and FG loop that are probable candidates for PSG binding to its putative ligand.
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- Zhou, G Q, et al.
(author)
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The carcinoembryonic antigen (CEA) gene family in non-human primates.
- 2001
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In: Gene. - 0378-1119 .- 1879-0038. ; 264:1, s. 105-12
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Journal article (peer-reviewed)abstract
- Carcinoembryonic antigen (CEA) is a tumor marker of wide clinical use though its function remains unknown. The CEA counterpart and some related macromolecules cannot be demonstrated in mice, thus prohibiting studies of CEA function by gene disruption strategies. In an attempt to find a relevant animal model for functional studies of CEA we have investigated the occurrence of CEA subgroup members in baboon and African green monkey at the genomic and mRNA levels. The investigation was focused on the characteristic immunoglobulin-variable region-like (IgV-like) N-terminal domain of the family members. Based on N-domain sequences 3 and 4 different CEA subgroup genes, respectively, were identified. One sequence in each monkey species corresponded to human CEACAM8, while it was not possible to assign an obvious human counterpart for the other N-domain sequences. However, studies of cDNAs from African green monkey COS-1 cells identified one of the sequences as CEACAM1. Expression of CEACAM1 mRNA and protein was upregulated by IFNgamma as has previously been demonstrated for human CEACAM1. Presence of GPI-linked CEA subgroup members in African green monkey was suggested by sequencing. Both monkey species would thus seem suitable for functional studies of selected CEA subgroup members.
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