keratin

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Related to Keratins: actin, hard keratin

keratin

 [ker´ah-tin]
a scleroprotein that is the principal constituent of epidermis, hair, nails, horny tissues, and the organic matrix of the enamel of the teeth. Its solution is sometimes used in coating pills when the latter are desired to pass through the stomach unchanged.

ker·a·tin

(ker'ă-tin),
Collective name for a group of proteins that form the intermediate filaments in epithelial cells. Keratins have a molecular weight between 40 kD and 68 kD and are separated one from another by electrophoresis and isoelectric focusing; thus separated, they are sequentially numbered from 1-20, and also subdivided into low, intermediate, and high molecular weight proteins. According to their isoelectric mobility they are either acidic or basic. In general, each acidic keratin protein has its basic equivalent with which it is paired to form the intermediate filaments; some keratin proteins, however, occur unpaired. Various epithelial cells contain different keratin proteins, in a tissue-specific manner. Antibodies to keratin proteins are widely used for histologic typing of tumors, and are especially useful for distinguishing carcinomas from sarcomas, lymphomas, and melanomas.
Synonym(s): ceratin, cytokeratin
[G. keras (kerat-), horn, + -in]

keratin

/ker·a·tin/ (ker´ah-tin) any of a family of scleroproteins that are the main constituents of epidermis, hair, nails, and horny tissues. The high-sulfur keratin polypeptides of ectodermally derived structures, e.g., hair and nails, are also called hard k's.

keratin

(kĕr′ə-tĭn)
n.
1. Any of a class of filamentous proteins that are abundant in the cytoskeleton of vertebrate epithelial cells and are the main constituents of the outer layer of skin and tough epidermal structures such as hair, nails, hooves, feathers, and claws.
2. Material composed principally of keratin proteins.

ke·rat′i·nous (kə-răt′n-əs) adj.

keratin

[ker′ətin]
Etymology: Gk, keras, horn
a fibrous sulfur-containing protein that is the primary component of the epidermis, hair, nails, enamel of the teeth, and horny tissue of animals. The protein is insoluble in most solvents, including gastric juice. For this reason, it is often used as a coating for pills that must pass through the stomach unchanged to be dissolved in the intestines.

ker·a·tin

(ker'ă-tin)
A scleroprotein or albuminoid present in hair and nails; it contains a relatively large amount of sulfur, is insoluble in gastric juice, and is sometimes used for coating tablets that are intended to be dissolved only in the intestine.
Synonym(s): cytokeratin.
[G. keras (kerat-), horn, + -in]

keratin

A hard protein (scleroprotein) of cylindrical, helical molecular form occurring in horny tissue such as hair and nails and in the outer layers of the skin. Hair and nails consist almost wholly of keratin. Keratins are insoluble and cannot generally be split by PROTEOLYTIC enzymes.

keratin

a hard, fibrous, sulphur-containing protein with an alpha-helix structure, found in the epidermis of vertebrates, mainly in the outermost layers of skin. Keratin can have several forms: in scales, feathers, hooves, horns, claws and nails it is hard, while wool and hair are made up of a soft and flexible form.

Keratin

A tough, nonwater-soluble protein found in the nails, hair, and the outermost layer of skin. Human hair is made up largely of keratin.

ker·a·tin

(ker'ă-tin)
Collective name for a group of proteins that form intermediate filaments in epithelial cells. Keratins have a molecular weight of 40-68 kD and are either acidic or basic. Antibodies to keratin proteins are widely used for histologic typing of tumors and are especially useful for distinguishing carcinomas from sarcomas, lymphomas, and melanomas.
[G. keras (kerat-), horn, + -in]

keratin

a scleroprotein which is the principal constituent of epidermis, hair, nails, horny tissues, and the organic matrix of the enamel of the teeth. Its solution is sometimes used in coating pills when the latter are desired to pass through the stomach unchanged.

keratin cyst
see horn cyst.
keratin pearl
see horn pearls.
keratin tag
see fibrovascular papilloma.

Patient discussion about keratin

Q. skins does excrete oil and keratin what exactly is the whitish cape up that you can squeeze out from underskin

A. It sounds like you refer to sebum, an oily substance secreted by (how surprising :) ) sebaceus glands attached to the hair root. It's important for the skin, although abnormal secretion of it may cause diseases such as acne.

You may read more here:
http://en.wikipedia.org/wiki/Sebum#Sebum

More discussions about keratin
References in periodicals archive ?
As previously reported in EBS, immunostaining for keratin 14 is positive, outlining areas of cleavage within the basal cell layer of the skin.
Isolation, identification and heavy metal tolerance of keratin degrading strain KRD1
Scientists have confirmed thatphosphorylation plays an important role in regulating the formation of keratin filament and cell cycle [25].
PC is caused due to keratin gene mutations involving KRT6a, KRT6b, KRT6c, KRT16, KRT17.
For many who have cosmetic problems that occur due to the decline in the body's keratin supply, the logical solution is to replace the essential keratin in the body.
Keratins also contribute to the barrier properties [80] and are associated with regulatory functions [81], forming a signaling network with kinases [82].
These keratin fragments are relatively easy to manufacture, making them good candidates for low-cost therapeutics, the researchers said.
Different types of keratins are distinguished according to various characteristics such as physicochemical properties or according to cells and tissues that produce certain keratin.
Keratin solution was extracted from the prepared hairs using modification Shindai method [16].
Keratins are components of intermediate filaments and play an essential role in cytoskeleton formation (Morley and Lane 1994).
1) In their article, Xu and colleagues reported that no staining of fibroblastic-type reticulum cells was seen in sentinel lymph nodes with the AE1/AE3 keratin cocktail (0/84 cases).
Of note, introduction of a proline residue at corresponding positions in K14 (186Val[approaches]Pro) and K17 (155Ile[approaches]Pro) rendered these keratins K16-like in their tetramer-forming properties.