Mup genes from other mammals also encode allergenic proteins, for example Fel d 4 is primarily produced in the submandibular salivary gland and is deposited onto dander as the cat grooms itself. A study found that 63% of cat allergic people have antibodies against the protein. Most had higher titres of antibodies against Fel d 4 than against Fel d 1, another prominent cat allergen.[14] Likewise, Equ c1 (Equus caballus allergen 1) is the protein product of a horse Mup gene that is found in the liver, sublingual and submaxillary salivary glands.[1][67] It is responsible for about 80% of the antibody response in patients who are chronically exposed to horse allergens.[67]
[edit] Metabolism
While the detection of Mups excreted by other animals has been well studied, the functional role in the producing animal is less clear. However, in 2009, Mups were shown to be associated with the regulation of energy expenditure in mice. Scientists found that genetically induced obese, diabetic mice produce thirty times less Mup RNA than their lean siblings.[68] When they delivered Mup protein directly into the bloodstream of these mice, they observed an increase in energy expenditure, physical activity and body temperature and a corresponding decrease in glucose intolerance and insulin resistance. They propose that Mups' beneficial effects on energy metabolism occurs by enhancing mitochondrial function in skeletal muscle.[68] A study found Mups were reduced in diet-induced obese mice. In this case, the presence of Mups in the bloodstream of mice restricted glucose production by directly inhibiting the expression of genes in the liver.[69]
[edit] See also
Portal-puzzle.svg MCB portal
* Cis-vaccenyl acetate, an insect aggression pheromone.
* Major histocompatibility complex, peptides also implicated in individual recognition in mice.
* Proteins produced and secreted by the liver.
Notes
1. ^ a b c d e f g h i j k l Logan DW, Marton TF, Stowers L (2008). "Species specificity in major urinary proteins by parallel evolution". PLoS ONE 3 (9): e3280. doi:10.1371/journal.pone.0003280. PMID 18815613.
2. ^ In that year Richard Bright first related kidney disease, later to become known as Bright's disease, with albuminous urine.
3. ^ Comper WD, Hilliard LM, Nikolic-Paterson DJ, Russo LM (December 2008). "Disease-dependent mechanisms of albuminuria". Am. J. Physiol. Renal Physiol. 295 (6): F1589–600. doi:10.1152/ajprenal.00142.2008. PMID 18579704.
4. ^ Lemley KV, Pauling L. (1994). "Thomas Addis: 1881–1949". Biographical Memoirs, National Academy of Sciences 63: 1–46.
http://books.nap.edu/openbook.php?record_id=4560&page=3.
5. ^ Addis T. (1932). "Proteinuria and cylinduria". Proceedings of the California Academy of Sciences 2: 38–52.
6. ^ Bell ME. (September 1933). "Albuminuria in the normal male rat". Journal of Physiology 79 (2): 191–93. PMID 16994453.
7. ^ Parfentjev IA, Perlzweig WA. (1933). "The Composition of the Urine of White Mice". The Journal of Biological Chemistry 100: 551–55.
http://www.jbc.org/content/100/2/557.full.pdf+html.
8. ^ a b Finlayson JS, Asofsky R, Potter M, Runner CC (August 1965). "Major urinary protein complex of normal mice: origin". Science 149 (687): 981–82. doi:10.1126/science.149.3687.981. PMID 5827345.
9. ^ a b c Roy AK, Neuhaus OW (March 1966). "Identification of rat urinary proteins by zone and immunoelectrophoresis". Proceedings of the Society for Experimental Biology and Medicine 121 (3): 894–99. PMID 4160706.
10. ^ a b Roy AK, Neuhaus OW (September 1966). "Proof of the hepatic synthesis of a sex-dependent protein in the rat". Biochimica et Biophysica Acta 127 (1): 82–87. doi:10.1016/0304-4165(66)90478-8. PMID 4165835.
11. ^ Held WA, Gallagher JF (April 1985). "Rat alpha 2u-globulin mRNA expression in the preputial gland". Biochemical Genetics 23 (3–4): 281–90. doi:10.1007/BF00504325. PMID 2409959.
12. ^ Gubits RM, Lynch KR, Kulkarni AB, et al. (October 1984). "Differential regulation of alpha 2u globulin gene expression in liver, lachrymal gland, and salivary gland". The Journal of Biological Chemistry 259 (20): 12803–809. PMID 6208189.
http://www.jbc.org/cgi/pmidlookup?view=long&pmid=6208189.
13. ^ Shahan K, Denaro M, Gilmartin M, Shi Y, Derman E (May 1987). "Expression of six mouse major urinary protein genes in the mammary, parotid, sublingual, submaxillary, and lachrymal glands and in the liver". Molecular and Cellular Biology 7 (5): 1947–54. PMID 3600653. PMC 365300.
http://mcb.asm.org/cgi/pmidlookup?view=long&pmid=3600653.
14. ^ a b Smith W, Butler AJ, Hazell LA, et al. (November 2004). "Fel d 4, a cat lipocalin allergen". Clinical and Experimental Allergy 34 (11): 1732–38. doi:10.1111/j.1365-2222.2004.02090.x. PMID 15544598.
15. ^ a b Loebel D, Scaloni A, Paolini S, et al. (September 2000). "Cloning, post-translational modifications, heterologous expression and ligand-binding of boar salivary lipocalin". The Biochemical Journal 350 (Pt 2): 369–79. doi:10.1042/0264-6021:3500369. PMID 10947950.
16. ^ Beynon RJ, Hurst JL (February 2003). "Multiple roles of major urinary proteins in the house mouse, Mus domesticus". Biochemical Society Transactions 31 (Pt 1): 142–46. doi:10.1042/BST0310142. PMID 12546672.
17. ^ Kurtz DT (1981). "Rat alpha 2u globulin is encoded by a multigene family". Journal of Molecular and Applied Genetics 1 (1): 29–38. PMID 6180115.
18. ^ Hastie ND, Held WA, Toole JJ (June 1979). "Multiple genes coding for the androgen-regulated major urinary proteins of the mouse". Cell 17 (2): 449–57. doi:10.1016/0092-8674(79)90171-5. PMID 88267.
19. ^ Bishop JO, Clark AJ, Clissold PM, Hainey S, Francke U (1982). "Two main groups of mouse major urinary protein genes, both largely located on chromosome 4". The EMBO Journal 1 (5): 615–20. PMID 6329695.