Specific Cleavage of the A1 Protein from Myelin with Cathepsin D

Brostoff, Steven W.; Reuter, W.; Hichens, Martin; Eylar, E.H.

doi:10.1016/s0021-9258(19)43066-4

Cited by 130 publications

(9 citation statements)

References 46 publications

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“…Two peptides CD1 and R, which comprise 77% of peptide L, have been shown to be encephalitogenic in the monkey (Brostoff et al, 1974;Kibler et al, 1972). However, Eylar et al (1972) observed that peptide R is tenfold less active than the carboxyl terminal region of the basic protein.…”

Section: Discussionmentioning

confidence: 99%

“…Two regions, found within the peptide L sequence, have been reported to be more active on a molar basis than peptide L (Figure 6). These peptides have been termed CDl and peptide R (Brostoff et al, 1974;Eylar et al, 1972;Kibler et al, 1972). The CDl peptide was obtained by Brostoff et al (1974) by treatment of the basic protein with cathepsin D. The cathepsin D cleaved the Phe-Phe bond of the basic protein between residues 43 and 44 giving rise to two peptides, CDl and CD2.…”

Section: Discussionmentioning

confidence: 99%

“…In the present communication we report the isolation and characterization of peptide L, containing 1% or less of basic protein, which shows weak encephalitogenic activity in the monkey. Since peptide L is comprised of peptides CD1 and R regions, the high activity on a molar basis observed by other workers (Brostoff et al, 1974 due to contamination of these peptides with the basic protein.…”

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confidence: 92%

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Allergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkey

Karkhanis¹,

Zeltner²,

Anderson³

et al. 1978

Biochemistry

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peptide L was further cleaved by cyanogen bromide, two peptides, peptide J (residues 1-20) and peptide D (residues 21-115), were obtained. Peptide J was inactive in inducing EAE, while peptide D was as weakly active as peptide L. Conformational studies and identical rate of tryptic hydrolysis Experimental allergic encephalomyelitis is an autoimmune disease induced by the basic protein of CNS* 1 myelin (Laatsch et al., 1962;Einstein et al., 1962; which comprises 30% of the total myelin protein. The protein is believed to have a highly ordered and folded structure and is best described as a prolate ellipsoid with an axial ratio 10:1 (Epand et al., 1974). The ease with which the basic protein can be isolated from myelin suggests that its location in the membrane is that of a so-called peripheral protein. The determination of the amino acid sequence of this protein has facilitated the definition of different encephalitogenic sites in this protein which are: a nonapeptide (residues 113-121

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 92%

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Allergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkey

Karkhanis¹,

Zeltner²,

Anderson³

et al. 1978

Biochemistry

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“…3 The numbering of residues of BP is based on the revised sequence data of 169 amino acid residues (16,37) in which the serine previously assigned to position 2 is absent. carbodiimide HCI were added, the solution was stirred at 25°C for 20 h and dialyzed at 4°C for 4 days against distilled H~O.…”

Section: Fragmentation Of Bp (Component 1)mentioning

confidence: 99%

Molecular internalization of a region of myelin basic protein

Whitaker¹,

Chou²,

Chou³

et al. 1977

The Journal of Experimental Medicine

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The conformation of myelin encephalitogenic or basic protein (BP) was investigated with a double-antibody radioimmunoassay by studying the reaction of BP or its fragments with antibodies produced in two rabbits against peptide 43-88 linked to rabbit serum albumin. Both antisera reacted well with peptide 43-88 but showed little or no reaction with BP. Absorption of these antisera with a BP-immunoadsorbent did not remove the antibody activity against peptide 43-88. Within the region of peptide 43- 88 it was shown that peptides 68-88 and 79-88 gave an equivalent or better reaction than peptide 43-88, whereas peptides 43-67 and 64-73 had very little reactivity. In the BP fragments containing region 43-88, peptide 1-88 showed the best reactivity, peptide 20-166 showed minimal reactivity, while peptide 1-115 showed none. These data document the internal position of at least a portion of peptide 43-88 and all of residues 79-88 in the BP molecule. The much greater reactivity of peptide 1-88 as compared to peptide 1-115 suggests that the region or a portion of the region of BP containing residues 89- 115 participates in the conformational alignment of BP restricting access to peptide 79-88. After absorption with BP, neither of the antisera prepared to peptide 43-88 reacted with PNS myelin in fixed tissue sections but continued to react with CNS myelin in similarly treated sections. The present findings demonstrate the need to consider the role of shielded antigenic determinants in the investigation of antigens or of immune responses.

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“…Ή εργασία των Marks et al (1974) καί των Brostoff et al (1974) δείχνει οτι ή περιορισμένη πρωτεόλυση της βασικής πρωτείνης της μυελίνης, ή όποια καταλύεται άπό τήν καθεψίνη D, ελευθερώνει πεπτίδια πού περιέχουν χαρακτηριστικές ανοσοποιητικές ομάδες οί όποιες μπορούν νά προκαλέσουν αλλεργική έγκεφαλομυελίτιδα. "Ετσι γεννάται τό ερώτημα κατά πόσο ή καθεψίνη D παίζει ρόλο στην παθογένεια της άπομυελινωτικής νόσου (Demyelinating disease).…”

Section: φυσιολογικός_ρόλος_τής_καθεψίνης^unclassified

Χημικη Τροποποιηση Της Καθεψινης D Με Διαιθυλοπυροκαρβονικο

Παπανδρεου-Ρακιτζη¹

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Specific Cleavage of the A1 Protein from Myelin with Cathepsin D

Cited by 130 publications

References 46 publications

Allergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkey

Allergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkey

Molecular internalization of a region of myelin basic protein

Χημικη Τροποποιηση Της Καθεψινης D Με Διαιθυλοπυροκαρβονικο

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