Lipocalins

Fig. 3.3 Lipocalins a generalised 3-D structure showing the p-barrel of eight sheets and the short a-helix (from Schofield, 1988).

Table 3.1 for the putative carriers in saliva, urine and nasal mucus the N-terminal sequences are highlighted against the pig salivary protein. All lipocalins or similar uncharacterised ( 20kDa) fractions with biological activity are extracellular, often found in quantity, 5 g/ml protein in male mouse urine and with a relatively high negative charge. 

The heterogeneity of the VN primary neurones is reflected in their modes of chemosensory preferences. The relative binding efficiencies for distinct odourant types onto the membrane sites is indeed functionally partitioned. When urinary fractions from male mice were applied to VN cells of females, stimulation by a lipophilic and volatile odourant fraction activated only the Gi protein-expressing cells. In contrast, Go activation was elicited by one of the lipocalin superfamily the MUP fraction containing an a-2-globulin (Krieger, 1999). This observation... 

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Loebel D., Scaloni A., Paolini S., Fini C., et al. (2000). Cloning, post-translational modifications, heterologous expression and ligand-binding of boar salivary lipocalin. Biochem J 350, 369-379. 

Marchese S., Pes D., Scaloni A., Carbone V. and Pelosi P. (1998). Lipocalins of boar salivary glands binding odours and pheromones. Europ J Biochem 252, 563-568. 

Miyawaki A., Matsushita F., Ryo Y. and Mikoshiba K. (1994). Possible pheromone-carrier function of 2 Lipocalin proteins in the vomeronasal organ. EMBO J 13, 5835-5842. 

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Scalfari F., Castagna M., Fattori B., Andreini I., et al. (1997). Expression of a lipocalin in human nasal mucosa. Comp Biochem Physiol B 118, 819-824. 

Thavathiru E., Jana N. and De P.K. (1999). Abundant secretory lipocalins displaying male and lactation-specific expression in adult hamster submandibular gland cDNA cloning and sex hormone-regulated repression. Eur J Biochem 266, 467-476. 

Achen, M. G., et al. (1992). Protein synthesis at the blood-brain barrier. The major protein secreted by amphibian choroid plexus is a lipocalin. J. Biol. Chem. 267, 23170-4. 

Beuckmann, C. T., et al. (2000). Cellular localization of lipocalin-type prostaglandin D synthase (beta-trace) in the central nervous system of the adult rat. J. Comp. Neurol 428, 62-78. 

Eguchi, Y., el at (1997). Expression of lipocalin-type prostaglandin D synthase... 

Eguchi, N., el at (1999). Lack of tactile pain (allodynia) in lipocalin-type... 

Fouchecourt, S., et at (2002a). Mammalian lipocalin-type prostaglandin D2 synthase in the fluids of the male genital tract putative biochemical and physiological functions. Biot Reprod. 66, 458-67. 

Fujimori, K, et at (2003). Regulation of lipocalin-type prostaglandin D synthase gene expression by Hes-1 through E-box and interleukin-1 beta via two NF-kappa B elements in rat leptomeningeal cells. ]. Biot Chem. 278, 6018-26. 

Fujimori, K, et at (2005). Protein kinase C activates human lipocalin-type... 

Garcia-Fernandez, L. F., et at (2000). Dexamethasone induces lipocalin-type... 

Gerena, R. L., et at (1998). Identification of a fertility-associated protein in bull seminal plasma as lipocalin-type prostaglandin D synthase. Biol Reprod. 58, 826-33. 

Gerena, R. L., et al. (2000a). Stage and region-specific localization of lipocalin-type prostaglandin D synthase in the adult murine testis and epididymis. J. Androl 21, 848-54. 

Irikura, D., et al. (2003). Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme. J. Biochem. 133, 29-32. 

Irikura, D., et at. (2007). Characterization of a major secretory protein in the cane toad (Bufo marinus) choroid plexus as an amphibian lipocalin-type prostaglandin D synthase. J. Biochem. 141, 173-80. 

Lepperdinger, G., el al. (1996). The lipocalin Xlcpll expressed in the neural plate of Xenopus laevis embryos is a secreted retinaldehyde binding protein. Protein Scl 5, 1250-60. 

Manya, H., et al. (2000). Comparative study of the asparagine-linked sugar chains of human lipocalin-type prostaglandin D synthase purified from urine and amniotic fluid, and recombinantly expressed in Chinese hamster ovary cells. 

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