Isolation, sequence, and developmental profile of a brain-specific polypeptide, PEP-19.

Ziai, R.; Pan, Yang; Hulmes, Jeffrey D.; Sangameswaran, Lakshmi; Morgan, James I.

doi:10.1073/pnas.83.21.8420

Cited by 88 publications

(76 citation statements)

References 36 publications

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“…1 depicts the examples of FTMS and MS/MS spectra for prohormone-derived peptide forms of VIP and pituitary adenylate cyclase-activating polypeptide (PACAP) identified with E-values of 9 ϫ 10 Ϫ16 and 2 ϫ 10 Ϫ27 , respectively. Although the sequence of VIP is HSDAVFTDNYTRLRKQMA-VKKYLNSI (AA 125-152), another peptide from the VIP prohormone was identified in this study: HSDAVFTDNYTRL (AA [125][126][127][128][129][130][131][132][133][134][135][136][137]. Because the observed peptide sequence results from cleavage of the prohormone at a dibasic cleavage site (RK), it appears to be a bona fide intracellular processing product from the VIP prohormone and is not expected to arise from extracellular degradation/processing.…”

Section: Resultsmentioning

confidence: 99%

Endogenous Peptide Discovery of the Rat Circadian Clock

Lee

Atkins

Hatcher

et al. 2010

Molecular & Cellular Proteomics

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Understanding how a small brain region, the suprachiasmatic nucleus (SCN), can synchronize the body's circadian rhythms is an ongoing research area. This important time-keeping system requires a complex suite of peptide hormones and transmitters that remain incompletely characterized. Here, capillary liquid chromatography and FTMS have been coupled with tailored software for the analysis of endogenous peptides present in the SCN of the rat brain. After ex vivo processing of brain slices, peptide extraction, identification, and characterization from tandem FTMS data with <5-ppm mass accuracy produced a hyperconfident list of 102 endogenous peptides, including 33 previously unidentified peptides, and 12 peptides that were post-translationally modified with amidation, phosphorylation, pyroglutamylation, or acetylation. This characterization of endogenous peptides from the SCN will aid in understanding the molecular mechanisms that mediate rhythmic behaviors in mammals. Molecular & Cellular Proteomics 9:285-297, 2010.

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Section: Resultsmentioning

confidence: 99%

Endogenous Peptide Discovery of the Rat Circadian Clock

Lee

Atkins

Hatcher

et al. 2010

Molecular & Cellular Proteomics

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“…Pep-19 (also known as Pcp4) is a 7.6-kDa IQ motif-containing protein (48) that is highly enriched in cerebellar Purkinje neurons (64). Structurally, Pep-19 belongs to the calpacitin protein family, which is characterized by homologous calmodulin (CaM)-binding (IQ motif) domains and includes RC3/ neurogranin, GAP-43/neuromodulin, Igloo, Pcp4L1, and SP17 (15,21,22).…”

mentioning

confidence: 99%

Impaired Locomotor Learning and Altered Cerebellar Synaptic Plasticity in pep-19/pcp4-Null Mice

Peng

Blundon

Rong

et al. 2011

Molecular and Cellular Biology

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“…The rodent cerebellum and, in particular, cerebellar Purkinje cells represent a tractable system with which to investigate biological processes and genetic regulatory factors critical in neurogenesis (1)(2)(3)(4)(5). Previous studies have been aimed at identifying genes that show specific or preferential expression in cerebellar Purkinje neurons (6)(7)(8)(9)(10)(11). Isolation and characterization of these genes will provide an understanding of the transcriptional strategies used in the central nervous system to generate and maintain diversity (5).…”

mentioning

confidence: 99%

Precerebellin is a cerebellum-specific protein with similarity to the globular domain of complement C1q B chain.

Urade

Oberdick

Molinar-Rode

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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104

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The cerebellum contains a hexadecapeptide, termed cerebellin, that is conserved in sequence from human to chicken. Three independent, overlapping cDNA clones have been isolated from a human cerebellum cDNA library that encode the cerebellin sequence. The longest clone codes for a protein of 193 amino acids that we term precerebellin. This protein has a significant similarity (31.3% identity, 52.2% similarity) to the globular (non-collagen-like) region of the B chain of human complement component Clq. The region of relatedness extends over =145 amino acids located in the carboxyl terminus of both proteins. Unlike Clq B chain, no collagen-like motifs are present in the amino-terminal regions of precerebellin. The amino terminus of precerebellin contains three possible N-linked glycosylation sites. Although hydrophobic amino acids are clustered at the amino terminus, they do not conform to the classical signal-peptide motif, and no other obvious membrane-spanning domains are predicted from the cDNA sequence. The cDNA predicts that the cerebellin peptide is flanked by Val-Arg and Glu-Pro residues. Therefore, cerebellin is not liberated from precerebellin by the classical dibasic amino acid proteolytic-cleavage mechanism seen in many neuropeptide precursors. In Northern (RNA) blots, precerebellin transcripts, with four distinct sizes (1.8, 2.3, 2.7, and 3.0 kilobases), are abundant in cerebellum. These transcripts are present at either very low or undetectable levels in other brain areas and extraneural structures. A similar pattern of cerebellin precursor transcripts are seen in rat, mouse, and human cerebellum. Furthermore, a partial genomic fragment from mouse shows the same bands in Northern blots as the human cDNA clone. During rat development, precerebellin transcripts mirror the level of cerebellin peptide. Low levels of precerebellin mRNA are seen at birth. Levels increase modestly from postpartum day 1 to 8, then increase more dramatically between day 5 and 15, and eventually reach peak values between day 21 and 56. Because cerebellin-like immunoreactivity is associated with Purki'ije cell postsynaptic structures, these data raise interesting possibilities concerning the function of the cerebellin precursor in synaptic physiology.

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Isolation, sequence, and developmental profile of a brain-specific polypeptide, PEP-19.

Abstract: By comparing the HPLC profiles of cerebellar extracts from adult and neonatal rats, a developmentally regulated polypeptide, termed PEP-19, was identified. The concentration of PEP-19 rose from 0

Cited by 88 publications

References 36 publications

Endogenous Peptide Discovery of the Rat Circadian Clock

Endogenous Peptide Discovery of the Rat Circadian Clock

Impaired Locomotor Learning and Altered Cerebellar Synaptic Plasticity in pep-19/pcp4-Null Mice

Precerebellin is a cerebellum-specific protein with similarity to the globular domain of complement C1q B chain.

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