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(Investigative Ophthalmology and Visual Science. 2000;41:3056-3060.)
© 2000 by The Association for Research in Vision and Ophthalmology, Inc.

Expression of ßB2-Crystallin mRNA and Protein in Retina, Brain, and Testis

Kristine S. Magabo1,2, Joseph Horwitz2,3, Joram Piatigorsky4 and Marc Kantorow1

From the 1 Department of Biology, West Virginia University, Morgantown, West Virginia; 2 The Jules Stein Eye Institute, University of California, Los Angeles Medical School; and 3 Laboratory of Molecular and Developmental Biology, National Eye Institute, Bethesda, Maryland.


   Abstract
Top
 Abstract
Introduction
 Methods
 Results
 Discussion
 References
 
PURPOSE. To evaluate the expression of ßB2-crystallin mRNA and protein in rat, bovine, and human nonlens and nonocular tissues.

METHODS. ßB2-crystallin mRNA levels were detected by RT-PCR. ßB2-crystallin protein was purified from rat and bovine tissues by FPLC chromatography. FPLC fractions were analyzed by immunoblotting. The identity of ßB2-crystallin protein, isolated from the retina, was confirmed by protein microsequencing.

RESULTS. ßB2-crystallin transcript was detected in rat brain, rat testis, and human retina by RT-PCR. ßB2-crystallin transcript was not found in rat lung, heart, ovary, spleen, thymus, kidney, and liver or in human brain and testis. ßB2-crystallin protein was partially purified from and its identity confirmed in rat brain, rat testis, and bovine retina. The bovine retinal protein was further confirmed to be authentic ßB2-crystallin by protein microsequencing.

CONCLUSIONS. These results establish that ßB2-crystallin mRNA and protein are expressed in tissues outside of the lens and outside of the eye including retina, brain, and testis. Extralenticular and extraocular expression of ßB2-crystallin, coupled with its participation in phosphorylation pathways, suggests that it has nonrefractive functions in these tissues.


   Introduction
Top
 Abstract
 Introduction
Methods
 Results
 Discussion
 References
 
The crystallin proteins that make up the transparent eye lens were originally thought to be restricted to the lens and to have entirely refractive functions. It is now established that several crystallins, including members of the {alpha}-, ß-, and {gamma}-crystallin gene families, are expressed outside of the lens where they may have nonrefractive functions.1 2 3 4 5 6 7 8 9 10 11 Indeed, both {alpha}A- and {alpha}B-crystallins are expressed in nonlens tissues1 2 4 5 and are functional chaperones that protect other proteins against thermal insult.12 13 {alpha}-Crystallins are also phosphorylated by cAMP-dependent14 15 and cAMP-independent16 17 18 pathways, suggesting that they may participate in signal transduction pathways.18

Like {alpha}-crystallin, ßB2-crystallin has also been detected outside of the lens.3 7 9 10 ßB2-crystallin protein has been reported in chicken retina,3 and ßB2-crystallin mRNA has been reported in rat brain, testis, lung, and other tissues.9 10 ßB2-crystallin is also involved in cAMP-dependent19 and cAMP-independent phosphorylation pathways.9 Extralenticular expression of ßB2-crystallin, coupled with its role in phosphorylation pathways, suggests that it may have an important nonrefractive function. To date, ßB2-crystallin protein has not been reported outside of the eye, and no information about its human nonlens expression is available. In the present report, we investigated the mRNA and protein expression patterns of ßB2-crystallin in rat, bovine, and human tissues. We show that both ßB2-crystallin mRNA and protein are present in nonlens and nonocular tissues.

The results support the possibility that ßB2-crystallin has one or more nonrefractive functions in nonocular tissues.


   Methods
Top
 Abstract
 Introduction
 Methods
Results
 Discussion
 References
 
Reverse Transcriptase PCR of ßB2-Crystallin
Three different procedures were used to amplify ßB2-crystallin mRNA. Rat Procedure: Total RNA from 3-day-old rat brain, testis, and lens was prepared using RNAzol (Tel-Test, Friendsworth, TX) as directed by the manufacturer. Ten or 2.0 µg of rat brain or testis and 2.0 µg of rat lens RNA were reverse-transcribed using mouse Moloney tumor virus reverse transcriptase (100 U/rxn; Gibco-BRL, Bethesda, MD) according to the manufacturer. Identical samples were prepared in the absence of reverse transcriptase as controls. After first-strand synthesis, PCR was performed for 30 cycles using Taq polymerase (Perkin-Elmer Cetus, Foster City, CA) as recommended by the manufacturer. The oligonucleotide sequences used in this procedure are shown in Table 1 as primer sets 3 and 4, annealing to exons 3 and 6, and 4 and 6, respectively. The resulting RT-PCR products were separated by electrophoresis on 1.0% gels and visualized by ethidium staining. In addition to the above, total RNA was also analyzed by isolation from 60- to 90-day-old rat tissues using RNAzol. Total RNA from rat testis was also obtained from Ambion, Inc. (Austin, TX). Reverse transcription and cDNA amplification (35 and 40 cycles) were then conducted with the One-Step RT-PCR System according to the manufacturer (Gibco-BRL), and identical reactions were performed with heat-inactivated reverse transcriptase as control. The oligonucleotides used in this procedure are shown in Table 1 as primer sets 1 and 2 and anneal to ßB2-crystallin exons 2 and 6. As control, ß-actin was coamplified in identical reactions. The sequence of the ß-actin primers were 5'OH-TCATGAAGTGTGACGTTGACATCCGT-3' + 5'OH-CCTAGAAGCATTTGCGGTGCACGATG-3'. Products were separated by electrophoresis on 0.8% gels and visualized by ethidium staining. To confirm the identity of the RT-PCR fragments, the lens and brain products were cloned and sequenced to ensure they represented authentic ßB2-crystallin. Human Procedure: ßB2-crystallin was reverse-transcribed and PCR-amplified for 40 cycles from human lens RNA (prepared as indicated above) or PCR-amplified for 40 cycles using purified total cDNA prepared from retina, brain, and testis. The retina, brain, and testis total cDNAs were a gift from Ignacio Rodriquez of the National Eye Institute. Total cDNA was amplified with Amplitaq polymerase according to the manufacturer (BRL). The oligonucleotide sequences used for this procedure are shown in Table 1 as primer pair 5. These primers anneal to exons 2 and 6 of the ßB2-crystallin mRNA. Control ß-actin transcripts were coamplified in identical reactions.


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  		Table 1. Oligonucleotide Sets Used for RT-PCR Amplification

 
Purification of ßB2-Crystallin Protein from Nonlens Tissues
Proteins were prepared and separated by FPLC chromatography on a Pharmacia HR-6 column (Uppsala, Sweden) as previously described.20 Fractions coeluting with purified bovine ßB2-crystallin were collected, and protein concentrations were determined by standard methods.

Immunoblotting of Purified ßB2-Crystallin Fractions
One to 2 µg of each FPLC fraction (above) was denatured by boiling in 10% SDS buffer [10% (w/v) SDS, 0.5 M Tris-HCl (pH 6.8), 5% (v/v) 2-mercaptoethanol, and 5% (v/v) glycerol], loaded onto 12.5% polyacrylamide SDS gels, and electrophoresed. After electrophoresis, the proteins were transferred (30 V for 1 hour in 12 mM Tris-HCl, 96 mM glycine, 15% methanol) to nitrocellulose filters. The resulting blot was fixed in 25% isopropanol/10% acetic acid for 1 hour, washed with PBS for 30 minutes, and blocked with 3% bovine serum albumin in PBS for 1 hour. The blot was then washed three times in TBS (10 mM Tris-HCl, 50 mM NaCl, pH 7.5) over 15 minutes and incubated for 1 hour at room temperature with 1:1000 ßB2-crystallin antibody in 1% bovine serum albumin in TBS. The blot was subsequently washed five times in TBS over a period of 1 hour. Immunoreactive ßB2-crystallin was visualized by using the ABC kit (Pierce Biochemicals, Rockford, IL) as described by the manufacturer.

Microsequencing
A bovine retinal protein fraction coeluting with purified ßB2-crystallin was separated on a 12.5% SDS-PAGE gel, electrophoretically transferred to nitrocellulose, stained with ponceau S, and excised. The resulting sample was digested with trypsin; peptides were separated by HPLC, and a single peptide was microsequenced.

William Lane at the Harvard Microchemistry Facility conducted the HPLC and microsequencing procedures. The resulting protein sequence was aligned with the reported rat, bovine, and human ßB2-crystallin sequences using Lasergene (ver. 5.1) software (DNAStar, Madison, WI) and further analyzed using the BLAST algorithm, National Library of Medicine (NIH, Bethesda, MD).


   Results
Top
 Abstract
 Introduction
 Methods
 Results
Discussion
 References
 
Detection of ßB2-Crystallin Transcript in Rat Testis and Brain by RT-PCR
Figure 1 A shows the 228-bp and Figure 1B the 373-bp ßB2-crystallin products generated with primer pairs 4 and 3 (Table 1) , respectively. Two and 10 µg total RNA (1x and 5x) were used in the RT-PCR procedure. With primer set 4 (Fig. 1A) , ßB2-crystallin mRNA was detected in brain (lanes 1 and 2), testis (lanes 3 and 4), and as control lens (lane 5). With primer set 3 (Fig. 1B) , very low amounts of ßB2-crystallin mRNA were detected in brain (lanes 6 and 7), whereas high levels of ßB2-crystallin mRNA were detected in testis (lanes 8 and 9) and lens (lane 10). To further confirm ßB2-crystallin expression in these tissues, fresh total RNA samples were prepared from 60- to 90-day-old rat lens, brain, lung, heart, testis, ovary, spleen, thymus, kidney, and liver and analyzed by RT-PCR with additional primer sets (Table 1 , oligo sets 1 and 2). Significant amounts of ßB2-crystallin were detected in brain, lens, and testis total RNA (Fig. 1C , lanes 1 and 2; Fig. 1D , lane 1). The lens band appeared weaker than that found for brain. This is likely the result of minor degradation of this sample as evidenced by the presence of a lower band in the lens lane (Fig. 1C , lane 1) and reduced levels of the corresponding ß-actin band (Fig. 1C , lane 2). All products were reverse transcriptase-specific, and representative control products from brain and lens were sequenced and confirmed to be authentic ßB2-crystallin (data not shown). ß-Actin transcript was detected at high levels in corresponding reactions (Fig. 1C , lanes 3 and 4; Fig. 1D , lane 2). ßB2-crystallin mRNA was not detected by RT-PCR in 1.0 µg (Table 1 , oligo set 1) or 1.4 µg (Table 1 , oligo set 2) total RNA from lung, heart, ovary, spleen, thymus, kidney, or liver (data not shown).



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  		Figure 1. RT-PCR of ßB2-crystallin mRNA in rat brain (Br), testis (Te), and lens (Le). (A) Ethidium bromide–stained gel showing the levels of ßB2-crystallin mRNA (228 bp) in 10 µg (5x) or 2.0 µg (1x) of rat brain (lanes 1 and 2), testis (lanes 3 and 4), and lens (lane 5). Total RNA was reverse transcribed and amplified for 30 PCR cycles using primer set 4 from Table 1 . (B) Ethidium bromide–stained gel showing the levels of ßB2-crystallin mRNA (373 bp) in 10 µg (5x) or 2.0 µg (1x) of rat brain (lanes 6 and 7), testis (lanes 8 and 9), and lens (lane 10). Total RNA was reverse transcribed and amplified for 30 PCR cycles using primer set 3 from Table 1 . (C) Ethidium bromide–stained gel showing the levels of ßB2-crystallin mRNA (524 bp) detected by reverse transcription followed by 40 RT-PCR cycles using 1.4 µg of rat lens (lane 1) and brain (lane 2) total RNA with primer set 2 from Table 1 . Indicated as control are the corresponding levels of ß-actin transcript (285 bp) produced with 0.14 µg of the same lens (lane 3) and brain (lane 4) RNAs amplified at 40 cycles after reverse transcription. (D) Ethidium bromide–stained gel showing the levels of ßB2-crystallin mRNA (710 bp) in 1 µg of rat testis (lane 1) at 35 PCR cycles using primer set 1 from Table 1 . Also shown as control is the corresponding level of ß-actin transcript (285 bp) in 1 µg of the same sample (lane 2) amplified at 35 cycles after reverse transcription.

 
Detection of ßB2-Crystallin Transcript in Human Retina
To determine whether parallel patterns of ßB2-crystallin expression extended to human tissues, ßB2-crystallin mRNA levels were examined in human retina, brain, testis, and lens. Total RNA (1 µg) was used for monitoring ßB2-crystallin mRNA in lens, and purified total cDNA was used for monitoring ßB2-crystallin transcript in retina (6 ng), brain (3 ng), and testis (3 ng). Because about 3% of total RNA is mRNA and reverse-transcriptase is not 100% efficient, this amount of total cDNA is at least equivalent to the 1.0 to 1.4 µg total RNA used in the rat studies. The primers used for this analysis are shown in Table 1 (oligo set 5). ßB2-crystallin was only detected in the retina (Fig. 2 , lane 2). Shown as control are ßB2-crystallin mRNA in lens (Fig. 2 , lane 1) and positive expression of ß-actin mRNA in all tissues (Fig. 2 , lanes 5–8).



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  		Figure 2. RT-PCR of ßB2-crystallin mRNA in human tissues. Ethidium bromide–stained gel showing the relative levels of ßB2-crystallin mRNA (524 bp) after reverse transcription and amplification for 40 PCR cycles in 1 µg human lens RNA (lane 1), 6 ng purified human retina cDNA (lane 2), 3 ng purified human brain cDNA (lane 3), and 3 ng purified human testis cDNA (lane 4). Also indicated are the levels of ß-actin transcripts (285 bp) in the same samples amplified under identical conditions (lanes 5 through 8). The primers for human ßB2-crystallin are shown in Table 1 as oligo set 5.

 
FPLC Elution Profile and Immunoblotting of Rat and Bovine Protein Extracts
To confirm that ßB2-crystallin protein was present in tissues where ßB2-crystallin mRNA was detected, protein extracts were prepared from the indicated tissues and partially purified by FPLC chromatography. Fractions coeluting as a dimer with purified bovine lens ßB2-crystallin (34 minutes, Fig. 3 ) were collected and 1 to 2 µg of each fraction analyzed by Western blot analysis with ßB2-crystallin–specific antibody. Figure 3 shows the elution profile, and Figure 4 shows the corresponding Western blot. A single 27-kDa immunoreactive band comigrating with purified ßB2-crystallin was detected in rat testis, rat brain, and bovine retina (Fig. 4 , lanes 3–5, respectively). Shown as control are purified bovine lens ßB2-crystallin (Fig. 4 , lane 1) and molecular weight standards (Fig. 4 , lane 2).



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  		Figure 3. FPLC elution profile of brain, testis, and retinal tissue extracts. Individual tissues and species are indicated. Fractions coeluting with dimeric purified bovine ßB2-crystallin (indicated at 34 minutes) were collected and further analyzed.

 


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  		Figure 4. Immunoblotting of purified ßB2-crystallin. Lane 1, purified bovine lens control (2 µg); lane 3, testis (2 µg); lane 4, brain (2 µg); and lane 5, retina (2 µg). Indicated are the positions of the 27-kDa reactive bands and the prestained molecular weight standards (lane 2).

 
The minor bands migrating above or below the purified ßB2-crystallin control are most likely due to slight degradation and cross-linking of the overloaded sample.

Microsequencing of ßB2-Crystallin from Bovine Retina
To further confirm the identity of ßB2-crystallin protein in bovine retina, bovine retinal protein extract was prepared. FPLC was purified as described above and separated by SDS-PAGE, and the major band comigrating with purified lens ßB2-crystallin was excised from the gel. The resulting gel slice was digested with trypsin, and the resulting peptides were separated by HPLC. One peptide was chosen for microsequencing. Its sequence was identical with that reported for the corresponding region (amino acids 172–190) of bovine lens ßB2-crystallin. The sequence of this peptide, aligned with bovine,21 human,22 and rat23 ßB2-crystallin is shown in Figure 5 .



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  		Figure 5. The amino acid sequence of the HPLC-purified peptide obtained from trypsin digestion of ßB2-crystallin purified from bovine retina (boxed). Indicated are the corresponding sequences of cow, human, and rat ßB2-crystallin. Numbers located above the sequences indicate the relative amino acid positions.

 

   Discussion
Top
 Abstract
 Introduction
 Methods
 Results
 Discussion
References
 
The present report shows that ßB2-crystallin protein and mRNA are expressed in the retina, brain, and testis of multiple species. ßB2-crystallin mRNA was detected in human retina, rat brain, and rat testis by RT-PCR. ßB2-crystallin protein was purified from and its identity confirmed by immunoblotting in bovine retina, rat brain, and rat testis protein extracts. The identity of bovine retinal ßB2-crystallin protein was further confirmed by microsequencing.

Differences in ßB2-crystallin expression were found between rat and human tissues. In rat, ßB2-crystallin transcript was detected in brain and testis, whereas in human, ßB2-crystallin transcript was detected only in the retina. We believe that these differences are species-specific; however, we cannot rule out the possibility that developmental or spatial expression differences could also be involved. The rat brain RNA preparation was made from cerebellum and brain stem, whereas the human brain RNA preparation was made from whole brain. Because specific subregions of human brain or testis are not available, further localization of ßB2-crystallin in these tissues will have to await the availability of these tissues.

The results of the present study are consistent with previous studies demonstrating expression of ßB2-crystallin protein in the retina of several species including rat.3 10 16 However, the results do not coincide with a previous study that failed to detect ßB2-crystallin mRNA in rat brain and failed to detect ßB2-crystallin protein outside of the eye.10 We do not know the reason for this discrepancy; however, it is likely to be related to the fact that ßB2-crystallin protein was not FPLC fractionated in this other study and that a blotting procedure instead of direct PCR monitoring was used to examine the ßB2-crystallin transcript. The potential nonrefractive function of ßB2-crystallin in the retina, brain, and testis is not known. One possibility is that it is related to signal transduction pathways because ßB2-crystallin is known to be phosphorylated by a cAMP-dependent pathway.16 Evidence has also been reported for non-cAMP–dependent phosphorylation of ßB2-crystallin.9 Whatever its function, the present data extend our knowledge of ßB2-crystallin expression to the retina, brain, and testis, and they suggest a nonrefractive function for ßB2-crystallin in these tissues.


   Acknowledgements
 
The authors thank Ignacio Rodriguez of the National Eye Institute, Paula Ousley and Rory Dunaway of the Lions Eye Bank of Oregon, John Hawse and Ashley Halstead of the Kantorow laboratory, Quingling Huang and Lin-lin Ding of the Horwitz laboratory, Barbara Norman of the Piatigorsky laboratory, and William Lane of the Harvard Microchemistry Facility.


   Footnotes
 
2 Both authors contributed equally to this work. Back

Supported in part by National Eye Institute Grants EY3897 (JH) and EY13022 (MK) and a Research to Prevent Blindness Senior Investigator Award (JH).

Submitted for publication April 11, 2000; revised May 22, 2000; accepted May 26, 2000.

Commercial relationships policy: N.

Corresponding author: Marc Kantorow, Department of Biology, 320 Brooks Hall, West Virginia University, Beechurst Avenue, Morgantown, WV 26505. mkantoro{at}wvu.edu


   References
Top
 Abstract
 Introduction
 Methods
 Results
 Discussion
 References
 

  1. Bhat, SP, Nagineni, CN (1989) {alpha}B subunit of lens-specific protein {alpha}-crystallin is present in other ocular and non-ocular tissues Biochem Biophys Res Commun 58,319-325
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  5. Sax, CM, Piatigorsky, J. (1994) Expression of the {alpha}-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues Adv Enzymol Related Areas Mol Biol 69,155-201[Medline][Order article via Infotrieve]
  6. Smolich, BD, Tarkington, SK, Saha, MS, Grainger, RM (1994) Xenopus {gamma}-crystallin gene expression: evidence that the {gamma}-crystallin gene family is transcribed in lens and nonlens tissues Mol Cell Biol 14,1355-1363[Abstract/Free Full Text]
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  8. Brunekreef, GA, van Genesen, ST, Destree, OHJ, Lubsen, NH (1997) Extralenticular expression of Xenopus laevis {alpha}-, ß-, and {gamma}-crystallin genes Invest Ophthalmol Vis Sci 38,2764-2771[Abstract/Free Full Text]
  9. Kantorow, M, Horwitz, J, Sergeev, Y, Hejtmancik, JF, Piatigorsky, J. (1997) Extralenticular expression, cAMP-dependent, and cAMP-independent phosphorylation of ßB2-crystallin [ARVO Abstract] Invest Ophthalmol Vis Sci 38(4),S205Abstract nr 998.
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  16. Kantorow, M, Piatigorsky, J. (1994) {alpha}-Crystallin/small heat-shock protein has autokinase activity Proc Natl Acad Sci USA 91,3112-3116[Abstract/Free Full Text]
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  18. Kantorow, M, Piatigorsky, J. (1998) Phosphorylations of {alpha} -crystallin Int J Biol Macromol 22,307-314[Medline][Order article via Infotrieve]
  19. Kleinman, NJ, Chiesa, R, Kolks, MA, Spector, A. (1988) Phosphorylation of ß-crystallin B2 (beta Bp) in the bovine lens J Biol Chem 263,14978-14983[Abstract/Free Full Text]
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J. Graw, A. Neuhauser-Klaus, J. Loster, and J. Favor
A 6-bp Deletion in the Crygc Gene Leading to a Nuclear and Radial Cataract in the Mouse
Invest. Ophthalmol. Vis. Sci., January 1, 2002; 43(1): 236 - 240.
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J. Graw, J. Löster, D. Soewarto, H. Fuchs, A. Reis, E. Wolf, R. Balling, and M. H. de Angelis
Aey2, a New Mutation in the {beta}B2-Crystallin-Encoding Gene of the Mouse
Invest. Ophthalmol. Vis. Sci., June 1, 2001; 42(7): 1574 - 1580.
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J. Graw, N. Klopp, J. Löster, D. Soewarto, H. Fuchs, J. Becker-Follmann, A. Reis, E. Wolf, R. Balling, and M. H. de Angelis
Ethylnitrosourea-Induced Mutation in Mice Leads to the Expression of a Novel Protein in the Eye and to Dominant Cataracts
Genetics, March 1, 2001; 157(3): 1313 - 1320.
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N. Klopp, J. Löster, and J. Graw
Characterization of a 1-bp Deletion in the {{gamma}}E-Crystallin Gene Leading to a Nuclear and Zonular Cataract in the Mouse
Invest. Ophthalmol. Vis. Sci., January 1, 2001; 42(1): 183 - 187.
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