The function and differential sorting of a family of aplysia prohormone processing enzymes

Chun, Jay; Körner, Judith; Kreiner, Thane; Scheller, Richard H.; Axel, Richard

doi:10.1016/0896-6273(94)90336-0

Cited by 54 publications

(45 citation statements)

References 37 publications

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“…PACE4 is not found at significant levels in a number of non-neuroendocrine tissues such as liver, kidney, spleen, lung, gastrointestinal tract, germ cells and submaxillary glands [13,16,17]. The Aplysia PACE4 homologue is localized to the secretory granules of bag cell neurons along with egg-laying hormone and the Aplysia PC1 homologue [19]. It has been proposed that PACE4 is crucial to β-cell-specific processing [18].…”

Section: Introductionmentioning

confidence: 99%

“…Third, the identity of furin as the only major endoprotease in the constitutive pathway has been questioned [60,62]. Fourth, endoprotease(s) in the constitutive pathway clearly participate in the processing of pro-nerve growth factor, Aplysia egg-laying hormone, pro-7B2 and proparathyroid hormone [19,33,[63][64][65].…”

Section: Biosynthesis Intracellular Routing and Secretion Of Pace4mentioning

confidence: 99%

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PACE4: a subtilisin-like endoprotease with unique properties

Mains

Berard

Denault

et al. 1997

Biochemical Journal

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PACE4 is one of the neuroendocrine-specific mammalian subtilisin-related endoproteases believed to function in the secretory pathway. The biosynthesis and secretion of PACE4 have been studied using transfected neuroendocrine and fibroblast cell lines, as well as primary pituitary cultures. ProPACE4 (approx. 106 kDa) is cleaved intracellularly before secretion of PACE4 (approx. 97 kDa); the N-terminal propeptide cleavage is accelerated in a truncated form of PACE4 lacking the Cys-rich C-terminal region (PACE4s). Neither PACE4 nor PACE4s is stored in regulated neuroendocrine secretory granules, whereas pro-opiomelanocortin-derived peptides and prohormone convertase 1 enter the regulated secretory pathway efficiently. The relatively slow cleavage of the proregion of proPACE4 in primary anterior pituitary cells, followed by rapid secretion of PACE4, is similar to the results for proPACE4 in transfected cell lines. The enzyme activity of PACE4 is distinct from furin and prohormone convertases, both in the marked sensitivity of PACE4 to inhibition by leupeptin and the relative insensitivity of PACE4 to inhibition by Ca2+ chelators and dithiothreitol; PACE4 is not inhibited by the α1-antitrypsin Portland variant that is very potent at inhibiting furin. The unique biosynthetic and enzymic patterns seen for PACE4 suggest a role for this neuroendocrine-specific subtilisin-like endoprotease outside the pathway for peptide biosynthesis.

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Section: Introductionmentioning

confidence: 99%

Section: Biosynthesis Intracellular Routing and Secretion Of Pace4mentioning

confidence: 99%

PACE4: a subtilisin-like endoprotease with unique properties

Mains

Berard

Denault

et al. 1997

Biochemical Journal

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“…In furins and PACE4, this domain is replaced by a cysteine-rich domain [1][2][3]. Recently, a Ser/Thr-rich segment composed of about 20 amino acid residues was found in Aplysia PC1A [7] and Aplysia furin2 [22]. The Ser/Thr-rich domain of Kex2 is thought to have Olinked oligosaccharide chains [23].…”

Section: Discussionmentioning

confidence: 99%

“…protease [8], and in mollusk Aplysia, five members of the kexin family including PC2-and furin-like enzymes have also been identified [7,22]. Thus, further studies will be required to elucidate a functional role of limulus kexins in horseshoe crab.…”

Section: Discussionmentioning

confidence: 99%

“…A number of Kex2-1ike proteases (kexin family) with different substrate specificities are present beyond species in eukaryotes such as mammals [1][2][3], insects [4][5][6], mollusks [7], cnidarians [8], and protochordates [9]. They are Ca2+-dependent serine proteases with a bacterial subtilisin-like catalytic domain and responsible for proteolytic processing of proproteins at dibasic sites.…”

Section: Introductionmentioning

confidence: 99%

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Limulus kexin: a new type of Kex2‐like endoprotease specifically expressed in hemocytes of the horseshoe crab

1996

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Molecular cloning of a cDNA encoding the neuropeptides APGWamide and cerebral peptide 1: Localization of APGWamide-like immunoreactivity in the central nervous system and male reproductive organs ofAplysia

Fan

Croll

et al. 1997

J. Comp. Neurol.

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While much is known about the neural and endocrine mechanisms that control egg laying in the gastropod mollusk Aplysia, relatively little is known about the regulation of male reproductive activity in this simultaneous hermaphrodite. In the present study, we have cloned and sequenced a cDNA that encodes a precursor protein, the predicted posttranslational processing of which presumably generates nine copies of the neuropeptide Ala-Pro-Gly-Trp-NH2 (APGWamide), five connecting peptide sequences, and a C-terminal peptide. The sequence of one connecting peptide is identical to the previously characterized cerebral peptide 1. Northern blot analysis identified two major APGWamide mRNA transcripts (approximately 1.3 kb, approximately 2.4 kb), which were present in central nervous system ganglia, but were most abundant in the right cerebral and right pedal ganglia. Immunohistochemical studies using sexually mature Aplysia demonstrated that the vast majority of APGWamide-like immunoreactivity was localized in 30-40 neurons along the anterior and medial margins of the right cerebral ganglion and in a cluster of 15-20 neurons in the right pedal ganglion. A total of only about ten immunoreactive neurons were located in other ganglia. Immunohistochemistry also demonstrated that APGWamide was present in the reproductive organs that participate in the storage or transport of sperm, including the small hermaphroditic duct (site of sperm storage before mating), the white hemiduct (also known as the copulatory duct), and penial complex. As a group, these data suggest that APGWamide may play a role in regulating male reproductive function in Aplysia, as it does in other gastropods.

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The function and differential sorting of a family of aplysia prohormone processing enzymes

Cited by 54 publications

References 37 publications

PACE4: a subtilisin-like endoprotease with unique properties

PACE4: a subtilisin-like endoprotease with unique properties

Limulus kexin: a new type of Kex2‐like endoprotease specifically expressed in hemocytes of the horseshoe crab

Molecular cloning of a cDNA encoding the neuropeptides APGWamide and cerebral peptide 1: Localization of APGWamide-like immunoreactivity in the central nervous system and male reproductive organs ofAplysia

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