Brain-specific clones

Liu, Q. R., Lopdz-Corcuera, B., Mandiyan, S., Nelson, H and Nelson, N. (1993) Cloning and expression of a spinal cord- and brain-specific glycine transporter with novel structural... 

Ni B, Rosteck PR, Jr., Nadi NS, Paul SM (1994) Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent inorganic phosphate cotransporter. Proc Natl Acad Sci USA 91 5607-5611. 

Okajima T, Eukumoto S, Ito H, Kiso M, Hirabayashi Y, Urano T, Eurukawa K (1999) Molecular cloning of brain-specific GDla synthase (ST6GalNAc V) containing CAG/ Glutamine repeats. J Biol Chem 274 30557— 30562... 

Subsequently, Tomiuk et al. [56] also concluded that the enzyme they had previously cloned (nSMase 1 in their nomenclature) was predominantly localized in the microsomal fraction (endoplasmic reticulum and Golgi). anti-nSMase 1 antibodies did not affect the nSMase activity in membrane fractions from murine brain [56], indicating that nSMase 1 was one of at least two mammalian nSMases. Indeed, shortly afterwards, the same group published the cloning and characterization of a 71 kDa mammalian brain-specific, Mg -dependent nSMase [57],... 

Bruno JF, Xu Y, Song J, Berelowitz M (1992) Molecular cloning and functional expression of a brain-specific somatostatin receptor. Proc Natl Acad Sci USA 89 11151-11155... 

Hofmann, K., Tomiuk, S., Wolff, G., and Stoffel, W. Cloning and characterization of the mammaUan brain-specific, Mg2-i--dependent neutral sphingomyelinase. Proc Natl Acad Sci USA 97 (2000) 5895-5900. 

Dopamine receptors are found primarily in brain, although they also exist in kidney [33]. Two subtypes of dopamine receptor were initially identified based primarily on differences in their drug specificities and signaling mechanisms. D receptors were found to stimulate adenylyl cyclase activity, while D2 receptors inhibited this enzyme (Fig. 12-6). Subsequently, multiple Dr and D2-like receptors were identified by molecular cloning (Table 12-3) [33], All dopamine receptor subtypes are... 

Protein kinase C (PKC) comprises the other major class of Ca2+-dependent protein kinases and is activated by Ca2+ in conjunction with DAG and phosphatidylserine (discussed in Ch. 20). Multiple forms of PKC have been cloned, and the brain is known to contain at least seven species of the enzyme. The variant forms of PKC exhibit different cellular distributions in the brain and different regulatory properties. For example, they differ in the relative ability of Ca2+ and DAG to activate them some require both Ca2+ and DAG, whereas others can be activated by DAG alone, apparently without an increase in cellular Ca2+ concentrations. However, these enzymes show similar substrate specificities and, as a result, are often considered isoforms. 

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