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Epidermal

Histamine AND histamine antagonists). It is formed from histidine by the enzyme L-histidine decarboxylase. In the periphery, histamine is stored ia mast cells, basophils, cells of the gastric mucosa, and epidermal cells. In the CNS, histamine is released from nerve cells and acts as a neurotransmitter. The actions of histamine ate terrninated by methylation and subsequent oxidation via the enzymes histamine-/V-methyltransferase and monoamine oxidase. [Pg.554]

Whereas epidermal growth factor (EGF) enhances the radiosensitivity of human squamous ceU carcinoma cells in vitro (197), addition of EGF to hormone-deprived MCE-7 breast cancer cells prior to irradiation results ia iacreased radioresistance (198). An anti-EGE-receptor monoclonal antibody blocks the abiUty of EGE to enhance growth and radioresistance. Tumor cells, the growth of which is stimulated by EGE, appear to be protected those where growth is iohibited are sensitized (198). [Pg.496]

There are hundreds of topical steroid preparations that are available for the treatment of skin diseases. In addition to their aforementioned antiinflammatory effects, topical steroids also exert their effects by vasoconstriction of the capillaries in the superficial dermis and by reduction of cellular mitosis and cell proliferation especially in the basal cell layer of the skin. In addition to the aforementioned systemic side effects, topical steroids can have adverse local effects. Chronic treatment with topical corticosteroids may increase the risk of bacterial and fungal infections. A combination steroid and antibacterial agent can be used to combat this problem. Additional local side effects that can be caused by extended use of topical steroids are epidermal atrophy, acne, glaucoma and cataracts (thus the weakest concentrations should be used in and around the eyes), pigmentation problems, hypertrichosis, allergic contact dermatitis, perioral dermatitis, and granuloma gluteale infantum (251). [Pg.446]

Emulsion components enter the stratum corneum and other epidermal layers at different rates. Most of the water evaporates, and a residue of emulsifiers, Hpids, and other nonvolatile constituents remains on the skin. Some of these materials and other product ingredients may permeate the skin others remain on the surface. If the blend of nonvolatiles materially reduces the evaporative loss of water from the skin, known as the transepidermal water loss (TEWL), the film is identified as occlusive. AppHcation of a layer of petrolatum to normal skin can reduce the TEWL, which is normally about 4—8 g/(m h), by as much as 50 to 75% for several hours. The evaporated water is to a large extent trapped under the occlusive layer hydrating or moisturizing the dead cells of the stratum corneum. The flexibiHty of isolated stratum corneum is dependent on the presence of water dry stratum corneum is britde and difficult to stretch or bend. Thus, any increase in the water content of skin is beHeved to improve the skin quaHty. [Pg.296]

Air pollutants may enter plant systems by either a primary or a secondary pathway. The primary pathway is analogous to human inhalation. Figure 8-2 shows the cross section of a leaf. Both of the outer surfaces are covered by a layer of epidermal cells, which help in moisture retention. Between the epidermal layers are the mesophyll cells—the spongy and palisade parenchyma. The leaf has a vascular bundle which carries water, minerals, and carbohydrates throughout the plant. Two important features shown in Fig. 8-2 are the openings in the epidermal layers called stomates, which are controlled by guard cells which can open and close, and air spaces in the interior of the leaf. [Pg.111]

These three functions involve the movement of O2, CO2, and HjO through the epidermal layers of the leaf. The analogy to human inhalation is obvious. With the diffusion of gases into and out of the leaf, pollutant gases have a direct pathway to the cellular system of the leaf structure. Direct deposition of particulate matter also occurs on the outer surfaces of the leaves. [Pg.112]

Figure 2.19 Organization of polypeptide chains into domains. Small protein molecules like the epidermal growth factor, EGF, comprise only one domain. Others, like the serine proteinase chymotrypsin, are arranged in two domains that are required to form a functional unit (see Chapter 11). Many of the proteins that are involved in blood coagulation and fibrinolysis, such as urokinase, factor IX, and plasminogen, have long polypeptide chains that comprise different combinations of domains homologous to EGF and serine proteinases and, in addition, calcium-binding domains and Kringle domains. Figure 2.19 Organization of polypeptide chains into domains. Small protein molecules like the epidermal growth factor, EGF, comprise only one domain. Others, like the serine proteinase chymotrypsin, are arranged in two domains that are required to form a functional unit (see Chapter 11). Many of the proteins that are involved in blood coagulation and fibrinolysis, such as urokinase, factor IX, and plasminogen, have long polypeptide chains that comprise different combinations of domains homologous to EGF and serine proteinases and, in addition, calcium-binding domains and Kringle domains.
Domains that are homologous to the epidermal growth factor, EGF, which is a small polypeptide chain of 53 amino acids. [Pg.29]

FIGURE 6.38 A sampling of proteins that consist of mosaics of individual protein modules. The modules shown include 7CG, a module containing 7-carboxyglutamate residues G, an epidermal growth-factor-like module K, the kringle domain, named for a Danish pastry ... [Pg.196]

These interactions involve adhesion proteins called selectins, which are found both on the rolling leukocytes and on the endothelial cells of the vascular walls. Selectins have a characteristic domain structure, consisting of an N-terminal extracellular lectin domain, a single epidermal growth factor (EGR) domain, a series of two to nine short consensus repeat (SCR) domains, a single transmembrane segment, and a short cytoplasmic domain. Lectin domains, first characterized in plants, bind carbohydrates... [Pg.283]

III. Tyr protein kinases A. Cytosolic tyrosine kinases src, fgr, abl, etc.) B. Receptor tyrosine kinases (RTKs) Plasma membrane receptors for hormones such as epidermal growth factor (EGF) or platelet-derived growth factor (PDGE) Raf (a protein kinase)... [Pg.467]

Investigation of cytotoxic antitumor activity of phthalocyanin conjugates with epidermal growth factor 98MI55. [Pg.233]

Oberhaut-. epidermic, epidermal. Ober-hMutchen, n. cuticle, -hefe, /. top yeast. [Pg.324]

The two isozymes are both homodimers, composed of approximately 600 amino acids and possess approximately 60% homology. The three-dimensional structures of COX-1 and COX-2 are very similar. Each one consists of three independent units an epidermal growth factor-like domain, a membrane-binding section and an enzymic domain. The catalytic sites and the residues immediately adjacent are identical but for two small but crucial variations that result in an increase in the volume of the COX-2-active site, enabling it to accept inhibitor-molecules larger than those that could be accommodated in the COX-1 molecule. [Pg.404]

The epidermal growth factor receptor 2 (HER-2) is a protein found on the surface of cells. Heterodimerization of HER-2 activates the enzyme tyrosine kinase, triggering reactions that cause the cells to grow and multiply. HER-2 is found at abnormally high levels on the surface of many types of cancer cells, which may divide excessively. Antibodies targeting HER-2 (e.g., trastuzumab) are used as antineoplastic agents. [Pg.478]

Epidermal Growth Factor Receptor Family Growth Factors... [Pg.482]

The regulation of NHE2 is multifactorial. Chronic exposure to nitric oxide and gamma-interferon decrease NHE2 activity, whereas metabolic acidosis and chronic stimulation with epidermal growth factor (EGF) increase activity. [Pg.810]


See other pages where Epidermal is mentioned: [Pg.221]    [Pg.277]    [Pg.272]    [Pg.281]    [Pg.282]    [Pg.428]    [Pg.159]    [Pg.113]    [Pg.290]    [Pg.292]    [Pg.834]    [Pg.88]    [Pg.118]    [Pg.107]    [Pg.156]    [Pg.370]    [Pg.436]    [Pg.457]    [Pg.474]    [Pg.478]    [Pg.478]    [Pg.478]    [Pg.478]    [Pg.478]    [Pg.497]    [Pg.505]    [Pg.565]    [Pg.566]    [Pg.604]    [Pg.604]    [Pg.706]    [Pg.709]    [Pg.742]   


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Allopurinol toxic epidermal necrolysis

Anti-epidermal growth factor

Atrophy, epidermal

BALB/c mice epidermal cell culture

Breast Cancer Human Epidermal Growth Factor Tyrosine Kinase Inhibitors

Breast cancer epidermal growth hormone receptor

Breast cancer human epidermal growth factor receptor

Breast tumors epidermal growth factor receptor

Calcium-binding epidermal growth factor

Cancer epidermal growth factor

Cancer epidermal growth hormone receptor

Cancer epidermal growth hormone receptor and

Cancer human epidermal growth factor

Carbamazepine toxic epidermal necrolysis

Chalone Epidermal

Chemical carcinogenesis studies in epidermal cell culture

Clearance, epidermal

Delayed drug reactions toxic epidermal necrolysis

Dimerization epidermal growth factor receptors

EGFR (epidermal growth factor

EGFR (epidermal growth factor breast cancer

EGFR (epidermal growth factor erlotinib gefitinib

EGFR (epidermal growth factor inhibitor selectivity

EGFR (epidermal growth factor kinase activation

EpiDerm

EpiDerm human skin model

Epidermal 0 transformation

Epidermal Growth Factor Receptor 2 (ErbB

Epidermal Vesicles

Epidermal alterations

Epidermal architecture

Epidermal barrier

Epidermal barrier homeostasis

Epidermal biochemical differentiation

Epidermal carcinoma

Epidermal cell culture

Epidermal cell proliferation

Epidermal cells

Epidermal cross /3-forms

Epidermal cytochrome

Epidermal differentiation

Epidermal differentiation complex (EDC

Epidermal elasticity

Epidermal extraction

Epidermal flavonoids

Epidermal gland

Epidermal growth factor

Epidermal growth factor (EGF)

Epidermal growth factor , receptor

Epidermal growth factor -derived

Epidermal growth factor -like domains, calcium-binding proteins

Epidermal growth factor Drosophila with

Epidermal growth factor amino-acid sequence

Epidermal growth factor and

Epidermal growth factor biological activities

Epidermal growth factor brain development

Epidermal growth factor carcinogenesis

Epidermal growth factor cell culture

Epidermal growth factor cell membrane binding

Epidermal growth factor cell-surface receptors

Epidermal growth factor cells

Epidermal growth factor cells targeted

Epidermal growth factor cellular mechanisms

Epidermal growth factor comparison

Epidermal growth factor cysteine richness

Epidermal growth factor decreased dependence

Epidermal growth factor family

Epidermal growth factor fluorescent

Epidermal growth factor interaction

Epidermal growth factor introduction

Epidermal growth factor ligand binding with

Epidermal growth factor ligand-induced dimerization

Epidermal growth factor mitogenicity

Epidermal growth factor modules

Epidermal growth factor precursor

Epidermal growth factor precursor homology domain

Epidermal growth factor radiosensitizer

Epidermal growth factor receptor (EGFR

Epidermal growth factor receptor , and

Epidermal growth factor receptor Drosophila with

Epidermal growth factor receptor EGER)

Epidermal growth factor receptor HeLa cells

Epidermal growth factor receptor Herceptin with

Epidermal growth factor receptor anti-HER2 antibodies with

Epidermal growth factor receptor cancer associated with

Epidermal growth factor receptor family

Epidermal growth factor receptor family targeting

Epidermal growth factor receptor gene

Epidermal growth factor receptor ligand binding

Epidermal growth factor receptor ligand-induced dimerization

Epidermal growth factor receptor ligand-induced signaling

Epidermal growth factor receptor ligands

Epidermal growth factor receptor mediated pathways, inhibition

Epidermal growth factor receptor molecular targeting

Epidermal growth factor receptor naming

Epidermal growth factor receptor oncogene

Epidermal growth factor receptor proliferation mechanisms

Epidermal growth factor receptor prostate cancer

Epidermal growth factor receptor signaling

Epidermal growth factor receptor signaling pathway

Epidermal growth factor receptor structure

Epidermal growth factor receptor structure/function

Epidermal growth factor receptor testing

Epidermal growth factor receptor therapeutic targeting

Epidermal growth factor receptor transactivation

Epidermal growth factor receptor tyrosine kinase

Epidermal growth factor receptor uniqueness

Epidermal growth factor receptor, cancer protection

Epidermal growth factor receptors EGFR mutants

Epidermal growth factor receptors biochemistry

Epidermal growth factor receptors cancer

Epidermal growth factor receptors interacting proteins

Epidermal growth factor receptors irreversible inhibitors

Epidermal growth factor receptors model

Epidermal growth factor receptors mutations

Epidermal growth factor structure/function

Epidermal growth factor subfamily

Epidermal growth factor therapy studies

Epidermal growth factor, murine

Epidermal growth factors ErbB binding

Epidermal growth factors ErbB signaling

Epidermal growth factors receptor, identification

Epidermal growth hormone receptor

Epidermal hairs

Epidermal hyaluronan

Epidermal hyperplasia

Epidermal keratinization

Epidermal keratinocytes

Epidermal layer/cells

Epidermal layers of skin

Epidermal lipids

Epidermal membranes

Epidermal molecular weight

Epidermal mucin

Epidermal mucus of fish

Epidermal necrosis

Epidermal ornithine decarboxylase activity

Epidermal photoreceptors

Epidermal physical properties

Epidermal polypeptide chains

Epidermal production

Epidermal proinflammatory cytokines

Epidermal purification

Epidermal reversibility

Epidermal sliding

Epidermal structure

Epidermal substitutes

Epidermal thickening

Epidermal thickness

Epidermal transglutaminase

Epidermal tumors

Epidermal turnover

Epidermal, outgrowths

Epidermal-Dermal Junction (Basement Membrane)

Epidermal-dermal junction

Epidermal-dermal junction components

Epidermal-dermal junction functions

Epidermic barrier

Estimation of Epidermal Growth Factor Receptor Expression

Fetal epidermal cells

HER2 (human epidermal growth

HER2 (human epidermal growth factor receptor

Heparin-binding epidermal growth factor

Heparin-binding epidermal growth factor HB-EGF)

Holocrine epidermal

Human epidermal growth

Human epidermal growth factor

Human epidermal growth factor coupling

Human epidermal growth factor receptor

Human epidermal growth factor receptor 2 (HER

Human epidermal growth factor requirements

Human epidermal keratinocytes

Human epidermal membrane

Intra-epidermal vesicles

Irritants epidermal damage

KB-16 (human oral epidermal

KB-16 (human oral epidermal carcinoma

Keratinous epidermal layer

Lamotrigine toxic epidermal necrolysis

Lipogenesis, epidermal

Melasma epidermal

Neural-epidermal interactions

Nevirapine toxic epidermal necrolysis

Normal human epidermal keratinocytes

Normal human epidermal keratinocytes NHEKs)

Oral epidermal carcinoma

Psoriasis epidermal proliferation

Receptors, for epidermal differentiation

Recombinant human epidermal

Recombinant human epidermal growth factor

Signal transduction epidermal growth factor

Skin tumors epidermal

Staphylococcus epidermitis

Stem epidermal cells

Sterols, epidermal

Structure of epidermal growth factor

Tissue epidermal

Tissue epidermal of plants

Toxic epidermal necrolysis

Toxic epidermal necrolysis allergic drug reaction

Toxic epidermal necrolysis carbamazepine-induced

Toxic epidermal necrolysis drug-related

Toxic epidermal necrolysis management

Toxic epidermal necrolysis syndrome

Toxic epidermal necrosis

Trans-epidermal water loss

Wounds epidermal healing

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