scholarly journals The complete sequence of human lens γs-crystallin

1995 ◽  
Vol 307 (2) ◽  
pp. 407-410 ◽  
Author(s):  
J B Smith ◽  
Z Yang ◽  
P Lin ◽  
Z Zaidi ◽  
A Abbasi ◽  
...  
Keyword(s):  
Peptide Sequencing ◽  
Complete Sequence ◽  
Human Lens ◽  
Cdna Sequencing ◽  
Lens Crystallins ◽  
Original Sequence ◽  
Bovine Sequence ◽  
Gamma S

The complete sequence of human gamma s-crystallin has been determined and confirmed using a combination of MS methods, peptide sequencing and cDNA sequencing. Regions 21-35 and 102-107, which were previously assumed to be the same as the bovine sequence, differ from the bovine sequence at residues 22, 28, 31 and 104. An additional six residues were also found to be different from the original sequence determined for Pakastani lenses. Whether these differences represent errors in the original sequence or two different sequences among human lens crystallins is not yet known.

Age-Related Changes in Human Lens Crystallins Identified by HPLC and Mass Spectrometry

1998 ◽  
Vol 67 (1) ◽  
pp. 21-30 ◽  
Author(s):  
ZHIXIANG MA ◽  
STACY R.A. HANSON ◽  
KIRSTEN J. LAMPI ◽  
LARRY L. DAVID ◽  
DAVID L. SMITH ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Human Lens ◽  
Lens Crystallins ◽  
Age Related ◽  
Age Related Changes

scholarly journals P 207 Bendazac decreases in vitro glycation of human lens crystallins

1995 ◽  
Vol 35 ◽  
pp. S194
Author(s):  
C. Marques ◽  
J.S. Ramalho ◽  
P. Pereira ◽  
M.C. Mota
Keyword(s):  
Human Lens ◽  
Lens Crystallins

Amino Acid Sequence of a Major Human Amelogenin Protein Employing Edman Degradation and cDNA Sequencing

1993 ◽  
Vol 72 (12) ◽  
pp. 1566-1572 ◽  
Author(s):  
J. Catalano-Sherman ◽  
A. Palmon ◽  
Y. Burstein ◽  
D. Deutsch
Keyword(s):  
Present Report ◽  
Complete Sequence ◽  
Edman Degradation ◽  
Cdna Sequencing ◽  
Cdna Sequences ◽  
Coding Regions ◽  
Major Class ◽  
Human Enamel ◽  
Sequencing Studies ◽  
Enamel Protein

The abundant hydrophobic, proline-glutamine, and histidine-rich (over 90%) amelogenins constitute the major class of proteins in forming extracellular enamel matrix. These are thought to play a major role in the structural organization and mineralization of developing enamel. The present report describes the successful sequencing of the major human amelogenin protein, by use of both Edman degradation and cDNA sequencing. When Edman degradation was used, over 75% of the primary structure of the protein was determined. This sequence was supplemented with cDNA sequencing studies, which revealed the predicted sequence of this protein. Together, they provide the complete sequence of an important human enamel protein. The information complements recent studies on bovine and human amelogenin genes. A comparison between the present results and the protein sequences predicted from the corresponding human amelogenin genomic coding regions and that of cDNA sequences of other species is described.

scholarly journals LP2, a differentiation-associated lipid-binding protein expressed in bovine lens

1996 ◽  
Vol 320 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Cynthia JAWORSKI ◽  
Graeme WISTOW
Keyword(s):  
Cellular Differentiation ◽  
Expression Patterns ◽  
Complete Sequence ◽  
Lipid Binding ◽  
Human Lens ◽  
Fatty Acid Binding Proteins ◽  
Lens Protein ◽  
Differentiation Markers ◽  
Fatty Acid Binding ◽  
Bovine Lens

A 13 kDa protein from bovine lens was identified and characterized by protein microsequencing and by rapid amplification of cDNA ends (RACE) PCR. Its complete sequence shows that this protein belongs to a family of fatty acid-binding proteins (FABPs), including myelin and adipocyte P2, that are associated with cellular differentiation. The bovine lens protein, designated LP2, shows very close similarity to human epidermal FABP (eFABP) and human eFABP was detected in human lens, suggesting that the two proteins might be orthologous. Reverse transcriptase–PCR (RT–PCR) was used to compare expression patterns of LP2 with those for actin and for the differentiation markers γB-crystallin and γs-crystallin in lens. Actin was most abundant in the relatively undifferentiated epithelial cells and decreased with lens cell differentiation. In contrast γB-crystallin and γs-crystallin were detected only in fibres (nuclear and cortical respectively). LP2 transcripts were detected most abundantly in fibre cells and apparently increased with cellular differentiation. Molecular modelling confirms that the sequence of LP2 fits the tertiary template of adipocyte P2 but reveals the presence of two close pairs of cysteine residues that might be susceptible to intramolecular disulphide bond formation under appropriate oxidizing conditions. LP2 is thus another potential target for oxidative stress during cataract formation in lens.

scholarly journals A native chemical chaperone in the human eye lens

2020 ◽  
Author(s):  
Eugene Serebryany ◽  
Sourav Chowdhury ◽  
Christopher N. Woods ◽  
David C. Thorn ◽  
Nicki E Watson ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Vision Loss ◽  
Human Lens ◽  
Lens Crystallins ◽  
Chemical Chaperone ◽  
Negative Stain ◽  
Molecular Mechanism Of Action ◽  
Redox Buffers ◽  
Rate Limiting

Cataract is one of the most prevalent protein aggregation disorders and still the most common cause of vision loss worldwide. The metabolically quiescent core region of the human lens lacks cellular or protein turnover; it has therefore evolved remarkable mechanisms to resist light-scattering protein aggregation for a lifetime. We now report that one such mechanism involves an unusually abundant lens metabolite, myo-inositol, suppressing aggregation of lens crystallins. We quantified aggregation suppression using our previously well-characterized in vitro aggregation assays of oxidation-mimicking human γD-crystallin variants and investigated myo-inositol's molecular mechanism of action using solution NMR, negative-stain TEM, differential scanning fluorometry, thermal scanning Raman spectroscopy, turbidimetry in redox buffers, and free thiol quantitation. Unlike many known chemical chaperones, myo-inositol's primary target was neither the native nor the unfolded state of the protein, nor the final aggregated state, but rather the rate-limiting bimolecular step on the aggregation pathway. Given recent metabolomic evidence that it is severely depleted in human cataractous lenses compared to age-matched controls, we suggest that maintaining or restoring healthy levels of myo-inositol in the lens may be a simple, safe, and globally accessible strategy to prevent or delay lens opacification due to age-onset cataract.

Spatial and temporal mapping of the age-related changes in human lens crystallins

1985 ◽  
Vol 41 (6) ◽  
pp. 745-758 ◽  
Author(s):  
M.J. McFall-Ngai ◽  
L.-L. Ding ◽  
L.J. Takemoto ◽  
J. Horwitz
Keyword(s):  
Human Lens ◽  
Lens Crystallins ◽  
Age Related ◽  
Age Related Changes

scholarly journals Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a rac/rhoGDI complex.

1996 ◽  
Vol 7 (3) ◽  
pp. 397-408 ◽  
Author(s):  
A J O'Sullivan ◽  
A M Brown ◽  
H N Freeman ◽  
B D Gomperts
Keyword(s):  
Mast Cells ◽  
Peptide Sequencing ◽  
Bovine Brain ◽  
Nucleotide Exchange ◽  
Permeabilized Cells ◽  
Guanine Nucleotide Exchange ◽  
Exchange Inhibitor ◽  
Streptolysin O ◽  
Gamma S ◽  
Brain Cytosol

Mast cells permeabilized by treatment with streptolysin-O in the presence of Ca2+ and GTP-gamma-S can secrete almost 100% of their contained N-acetyl-beta-D-glucosaminidase. If these stimuli are provided to the permeabilized cells after a delay, the response is diminished and the ability of the cells to undergo secretion runs down progressively over a period of about 30 min. This is thought to be due to the loss of key proteins involved in the exocytotic mechanism. Using this effect as the basis of a biological assay, we have isolated a protein from bovine brain cytosol that retards the loss of responsiveness to stimulation by Ca2+ and GTP-gamma-S. Purification of this protein and peptide sequencing have enabled us to identify it as the small GTP-binding protein rac complexed to the guanine nucleotide exchange inhibitor rhoGDI. Both proteins are required to retard the loss of the secretory response, while purified rhoGDI applied alone accelerates the rundown.

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