Specific Tear Prealbumin: a Unique Lachrymal Protein absent from Serum and other Secretions

Bonavida, Benjamin; Sapse, A.T.; Sercarz, Eli E.

doi:10.1038/221375a0

Cited by 43 publications

(12 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, preliminary binding studies between the recombinant Tlc and Zn(II) revealed a rather weak dissociation constant of ϳ1.33 mM (determined as half-maximal metal ion concentration to achieve saturation during CD titration at 212 nm). 2 The unusual shape of the binding pocket of Tlc prompted us to investigate possible modes of interaction with two of its known ligands, retinoic acid and rifampin (7,15). Unfortunately, corresponding co-crystallization trials remained unsuccessful.…”

Section: Resultsmentioning

confidence: 99%

“…Tear lipocalin (Tlc, 1 also called Lcn1 or von Ebner's gland protein) was originally described as a unique major component of human tear fluid, comprising 15-33% of its protein content and secreted by the lacrimal glands (1,2). Later on it was also found to be produced by a number of other secretory glands and tissues, including lingual glands, nasal mucosal glands, secretory glands of the tracheobronchial tract, sweat glands, mammary gland, adrenal gland, prostate, thymus, testis, and by corticotrophs of the pituitary gland (3)(4)(5)(6).…”

mentioning

confidence: 99%

See 1 more Smart Citation

The 1.8-Å Crystal Structure of Human Tear Lipocalin Reveals an Extended Branched Cavity with Capacity for Multiple Ligands

Breustedt

Korndörfer

Redl

et al. 2005

Journal of Biological Chemistry

106

149

View full text Add to dashboard Cite

In contrast with earlier assumptions, which classified human tear lipocalin (Tlc) as an outlier member of the lipocalin protein family, the 1.8-Å resolution crystal structure of the recombinant apoprotein confirms the typical eight-stranded antiparallel ␤-barrel architecture with an ␣-helix attached to it. The fold of Tlc most closely resembles the bovine dander allergen Bos d 2, a well characterized prototypic lipocalin, but also reveals similarity with ␤-lactoglobulin. However, compared with other lipocalin structures Tlc exhibits an extremely wide ligand pocket, whose entrance is formed by four partially disordered loops. The cavity deeply extends into the ␤-barrel structure, where it ends in two distinct lobes. This unusual structural feature explains the known promiscuity of Tlc for various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampin and even to microbial siderophores. Notably, earlier findings of biological activity as a thiol protease inhibitor have no correspondence in the three-dimensional structure of Tlc, rather it appears that its proteolytic fragments could be responsible for this phenomenon. Hence, the present structural analysis sheds new light on the ligand binding activity of this functionally obscure but abundant human lipocalin.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

The 1.8-Å Crystal Structure of Human Tear Lipocalin Reveals an Extended Branched Cavity with Capacity for Multiple Ligands

Breustedt

Korndörfer

Redl

et al. 2005

Journal of Biological Chemistry

106

149

View full text Add to dashboard Cite

show abstract

“…Lactoferrin, a metal-binding protein, is present in large quantities and its role is thought to be a complexing one (2). Another specific protein, the 'specific tear prealbumin' studied by Bonavida et al (1), migrates more anodally than serum albumin in acrylamide gel electrophoresis under conditions used for the separation of acidic proteins.…”

Section: Introductionmentioning

confidence: 99%

Human Tears: Electrophoretic Characteristics of Specific Proteins

Gachon¹,

Lambin²,

Dastugue³

1980

Ophthalmic Res

View full text Add to dashboard Cite

Tear-specific proteins have been investigated. Protein with a relative mobility higher than that of albumin in non-denaturing electrophoresis has been shown to be highly heterogeneous. It is composed of at least six proteins, some of them being probably multimeric proteins. Their isoelectric points and the apparent molecular weights of their subunits have been estimated. Another tear-specific protein was found. Its molecular weight is 31,000 daltons and it is dissociated in the presence of reducing agents.

show abstract

“…Bonavida et al [2] suggest that At protein is synthesized only in the lacrimal gland. RTP-2 protein also clearly migrated faster than serum albumin.…”

mentioning

confidence: 99%

“…The At protein migrates faster toward the anode than does serum albumin [2], and it has not been identified in such body fluids as serum, spinal fluid, saliva or urine [7]. Bonavida et al [2] suggest that At protein is synthesized only in the lacrimal gland.…”

mentioning

confidence: 99%