21.06.2013 Views

Ganong's Review of Medical Physiology, 23rd Edition

Ganong's Review of Medical Physiology, 23rd Edition

Ganong's Review of Medical Physiology, 23rd Edition

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

Extracellular fluid<br />

Carbohydrate<br />

portion <strong>of</strong><br />

glycoprotein<br />

Channel<br />

Intregral<br />

proteins<br />

Nonpolar regions<br />

Transmembrane<br />

proteins<br />

Polar regions<br />

Peripheral<br />

protein<br />

Intracellular fluid<br />

FIGURE 2–2 Organization <strong>of</strong> the phospholipid bilayer and<br />

associated proteins in a biological membrane. The phospholipid<br />

molecules each have two fatty acid chains (wavy lines) attached to a phosphate<br />

head (open circle). Proteins are shown as irregular colored globules.<br />

Many are integral proteins, which extend into the membrane, but peripheral<br />

proteins are attached to the inside or outside (not shown) <strong>of</strong> the<br />

membrane. Specific protein attachments and cholesterol commonly<br />

found in the bilayer are omitted for clarity. (Reproduced with permission from<br />

Widmaier EP, Raff H, Strang K: Vander’s Human <strong>Physiology</strong>: The Mechanisms <strong>of</strong> Body<br />

Function, 11th ed. McGraw-Hill, 2008.)<br />

transporting ions across the membrane. Other proteins function<br />

as carriers, transporting substances down electrochemical<br />

CHAPTER 2 Overview <strong>of</strong> Cellular <strong>Physiology</strong> in <strong>Medical</strong> <strong>Physiology</strong> 33<br />

Phospholipids<br />

gradients by facilitated diffusion. Still others are ion channels,<br />

which, when activated, permit the passage <strong>of</strong> ions into or out <strong>of</strong><br />

the cell. The role <strong>of</strong> the pumps, carriers, and ion channels in<br />

transport across the cell membrane is discussed below. Proteins<br />

in another group function as receptors that bind ligands or<br />

messenger molecules, initiating physiologic changes inside the<br />

cell. Proteins also function as enzymes, catalyzing reactions at<br />

the surfaces <strong>of</strong> the membrane. Examples from each <strong>of</strong> these<br />

groups are discussed later in this chapter.<br />

The uncharged, hydrophobic portions <strong>of</strong> the proteins are<br />

usually located in the interior <strong>of</strong> the membrane, whereas the<br />

charged, hydrophilic portions are located on the surfaces.<br />

Peripheral proteins are attached to the surfaces <strong>of</strong> the membrane<br />

in various ways. One common way is attachment to glycosylated<br />

forms <strong>of</strong> phosphatidylinositol. Proteins held by<br />

these glycosylphosphatidylinositol (GPI) anchors (Figure<br />

2–3) include enzymes such as alkaline phosphatase, various<br />

antigens, a number <strong>of</strong> cell adhesion molecules, and three proteins<br />

that combat cell lysis by complement. Over 45 GPIlinked<br />

cell surface proteins have now been described in<br />

humans. Other proteins are lipidated, that is, they have specific<br />

lipids attached to them (Figure 2–3). Proteins may be<br />

myristolated, palmitoylated, or prenylated (ie, attached to<br />

geranylgeranyl or farnesyl groups).<br />

The protein structure—and particularly the enzyme content—<strong>of</strong><br />

biologic membranes varies not only from cell to cell,<br />

but also within the same cell. For example, some <strong>of</strong> the enzymes<br />

embedded in cell membranes are different from those in mitochondrial<br />

membranes. In epithelial cells, the enzymes in the<br />

cell membrane on the mucosal surface differ from those in the<br />

FIGURE 2–3 Protein linkages to membrane lipids. Some are linked by their amino terminals, others by their carboxyl terminals. Many are attached<br />

via glycosylated forms <strong>of</strong> phosphatidylinositol (GPI anchors). (Reproduced with permission from Fuller GM, Shields D: Molecular Basis <strong>of</strong> <strong>Medical</strong> Cell Biology.<br />

McGraw-Hill, 1998.)<br />

Lipid membrane Cytoplasmic or external face <strong>of</strong> membrane<br />

O<br />

N-Myristoyl<br />

N<br />

H<br />

Gly Protein COOH<br />

S-Palmitoyl<br />

Geranylgeranyl<br />

Farnesyl<br />

GPI anchor<br />

C<br />

C<br />

(Glycosylphosphatidylinositol)<br />

O<br />

S-Cys<br />

Protein<br />

S-Cys Protein NH2 S-Cys Protein NH2 O<br />

C CH 2<br />

C<br />

O<br />

CH<br />

C<br />

H 2<br />

O O<br />

O P O Inositol O C<br />

O<br />

NH 2<br />

Hydrophobic domain Hydrophilic domain<br />

Protein

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!